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Database: UniProt
Entry: Q9UKN5
LinkDB: Q9UKN5
Original site: Q9UKN5 
ID   PRDM4_HUMAN             Reviewed;         801 AA.
AC   Q9UKN5; Q9UFA6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 3.
DT   26-NOV-2014, entry version 132.
DE   RecName: Full=PR domain zinc finger protein 4;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 4;
GN   Name=PRDM4; Synonyms=PFM1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10552934; DOI=10.1006/geno.1999.5967;
RA   Yang X.-H., Huang S.;
RT   "PFM1 (PRDM4), a new member of the PR-domain family, maps to a tumor
RT   suppressor locus on human chromosome 12q23-q24.1.";
RL   Genomics 61:319-325(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-801.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 390-540.
RG   Structural genomics consortium (SGC);
RT   "The crystal structure of methyltransferase domain of human PR domain-
RT   containing protein 4.";
RL   Submitted (AUG-2008) to the PDB data bank.
CC   -!- FUNCTION: May function as a transcription factor involved in cell
CC       differentiation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues. Highly expressed in
CC       ovary, testis, pancreas, brain, heart and prostate.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 SET domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
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DR   EMBL; AF144757; AAD55249.2; -; mRNA.
DR   EMBL; BC035581; AAH35581.1; -; mRNA.
DR   EMBL; AL133083; CAB61401.1; -; mRNA.
DR   CCDS; CCDS9115.1; -.
DR   PIR; T42688; T42688.
DR   RefSeq; NP_036538.3; NM_012406.3.
DR   UniGene; Hs.506655; -.
DR   PDB; 2L9Z; NMR; -; A=366-402.
DR   PDB; 3DB5; X-ray; 2.15 A; A/B=390-540.
DR   PDBsum; 2L9Z; -.
DR   PDBsum; 3DB5; -.
DR   ProteinModelPortal; Q9UKN5; -.
DR   SMR; Q9UKN5; 365-751.
DR   BioGrid; 116288; 10.
DR   IntAct; Q9UKN5; 3.
DR   MINT; MINT-1183894; -.
DR   STRING; 9606.ENSP00000228437; -.
DR   PhosphoSite; Q9UKN5; -.
DR   DMDM; 25008960; -.
DR   MaxQB; Q9UKN5; -.
DR   PaxDb; Q9UKN5; -.
DR   PRIDE; Q9UKN5; -.
DR   DNASU; 11108; -.
DR   Ensembl; ENST00000228437; ENSP00000228437; ENSG00000110851.
DR   GeneID; 11108; -.
DR   KEGG; hsa:11108; -.
DR   UCSC; uc001tmp.3; human.
DR   CTD; 11108; -.
DR   GeneCards; GC12M108126; -.
DR   HGNC; HGNC:9348; PRDM4.
DR   HPA; HPA024322; -.
DR   MIM; 605780; gene.
DR   neXtProt; NX_Q9UKN5; -.
DR   PharmGKB; PA33716; -.
DR   eggNOG; COG5048; -.
DR   GeneTree; ENSGT00770000120502; -.
DR   HOGENOM; HOG000060213; -.
DR   HOVERGEN; HBG053672; -.
DR   InParanoid; Q9UKN5; -.
DR   KO; K12463; -.
DR   OMA; VLEFCII; -.
DR   OrthoDB; EOG7R830T; -.
DR   PhylomeDB; Q9UKN5; -.
DR   TreeFam; TF332513; -.
DR   Reactome; REACT_13695; p75NTR negatively regulates cell cycle via SC1.
DR   EvolutionaryTrace; Q9UKN5; -.
DR   GenomeRNAi; 11108; -.
DR   NextBio; 42234; -.
DR   PRO; PR:Q9UKN5; -.
DR   Bgee; Q9UKN5; -.
DR   CleanEx; HS_PRDM4; -.
DR   ExpressionAtlas; Q9UKN5; baseline and differential.
DR   Genevestigator; Q9UKN5; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0045786; P:negative regulation of cell cycle; TAS:Reactome.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   Gene3D; 3.30.160.60; -; 6.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   InterPro; IPR017124; Znf_PRDM4.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   PIRSF; PIRSF037161; PRDM4; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    801       PR domain zinc finger protein 4.
FT                                /FTId=PRO_0000047760.
FT   DOMAIN      412    529       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     545    566       C2H2-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     618    640       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     646    668       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     674    696       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     702    724       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     730    752       C2H2-type 6; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   CONFLICT     16     16       E -> A (in Ref. 1; AAD55249).
FT                                {ECO:0000305}.
FT   CONFLICT    580    580       H -> I (in Ref. 1; AAD55249).
FT                                {ECO:0000305}.
FT   CONFLICT    608    608       H -> Y (in Ref. 1; AAD55249).
FT                                {ECO:0000305}.
FT   CONFLICT    662    663       ES -> GV (in Ref. 1; AAD55249).
FT                                {ECO:0000305}.
FT   STRAND      374    377       {ECO:0000244|PDB:2L9Z}.
FT   HELIX       378    380       {ECO:0000244|PDB:2L9Z}.
FT   STRAND      382    388       {ECO:0000244|PDB:2L9Z}.
FT   TURN        389    391       {ECO:0000244|PDB:2L9Z}.
FT   HELIX       405    408       {ECO:0000244|PDB:3DB5}.
FT   STRAND      414    418       {ECO:0000244|PDB:3DB5}.
FT   STRAND      425    431       {ECO:0000244|PDB:3DB5}.
FT   STRAND      445    447       {ECO:0000244|PDB:3DB5}.
FT   STRAND      462    468       {ECO:0000244|PDB:3DB5}.
FT   STRAND      471    477       {ECO:0000244|PDB:3DB5}.
FT   TURN        481    483       {ECO:0000244|PDB:3DB5}.
FT   HELIX       486    489       {ECO:0000244|PDB:3DB5}.
FT   TURN        496    498       {ECO:0000244|PDB:3DB5}.
FT   STRAND      501    506       {ECO:0000244|PDB:3DB5}.
FT   STRAND      509    516       {ECO:0000244|PDB:3DB5}.
FT   STRAND      525    528       {ECO:0000244|PDB:3DB5}.
SQ   SEQUENCE   801 AA;  87920 MW;  13B9B94F0825D113 CRC64;
     MHHRMNEMNL SPVGMEQLTS SSVSNALPVS GSHLGLAASP THSAIPAPGL PVAIPNLGPS
     LSSLPSALSL MLPMGIGDRG VMCGLPERNY TLPPPPYPHL ESSYFRTILP GILSYLADRP
     PPQYIHPNSI NVDGNTALSI TNNPSALDPY QSNGNVGLEP GIVSIDSRSV NTHGAQSLHP
     SDGHEVALDT AITMENVSRV TSPISTDGMA EELTMDGVAG EHSQIPNGSR SHEPLSVDSV
     SNNLAADAVG HGGVIPMHGN GLELPVVMET DHIASRVNGM SDSALSDSIH TVAMSTNSVS
     VALSTSHNLA SLESVSLHEV GLSLEPVAVS SITQEVAMGT GHVDVSSDSL SFVSPSLQME
     DSNSNKENMA TLFTIWCTLC DRAYPSDCPE HGPVTFVPDT PIESRARLSL PKQLVLRQSI
     VGAEVGVWTG ETIPVRTCFG PLIGQQSHSM EVAEWTDKAV NHIWKIYHNG VLEFCIITTD
     ENECNWMMFV RKARNREEQN LVAYPHDGKI FFCTSQDIPP ENELLFYYSR DYAQQIGVPE
     HPDVHLCNCG KECNSYTEFK AHLTSHIHNH LPTQGHSGSH GPSHSKERKW KCSMCPQAFI
     SPSKLHVHFM GHMGMKPHKC DFCSKAFSDP SNLRTHLKIH TGQKNYRCTL CDKSFTQKAH
     LESHMVIHTG EKNLKCDYCD KLFMRRQDLK QHVLIHTQER QIKCPKCDKL FLRTNHLKKH
     LNSHEGKRDY VCEKCTKAYL TKYHLTRHLK TCKGPTSSSS APEEEEEDDS EEEDLADSVG
     TEDCRINSAV YSADESLSAH K
//
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