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Database: UniProt
Entry: Q9H4Q4
LinkDB: Q9H4Q4
Original site: Q9H4Q4 
ID   PRD12_HUMAN             Reviewed;         367 AA.
AC   Q9H4Q4; A3KFK9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   10-APR-2019, entry version 152.
DE   RecName: Full=PR domain zinc finger protein 12;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 12;
GN   Name=PRDM12; Synonyms=PFM9;
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].
RA   Yang X.-H., Huang S.;
RT   "A family of novel PR-domain (PRDM) genes as candidate tumor
RT   suppressors.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 60-229.
RG   Structural genomics consortium (SGC);
RT   "The crystal structure of methyltransferase domain of human PR domain-
RT   containing protein 12.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POLYMORPHISM,
RP   INVOLVEMENT IN HSAN8, VARIANTS HSAN8 TYR-31; ASN-102; CYS-160;
RP   CYS-168; ASP-172; LEU-289 AND POLY-ALA-352 INS, AND CHARACTERIZATION
RP   OF VARIANTS HSAN8 TYR-31; ASN-102; CYS-160; CYS-168; ASP-172; LEU-289
RP   AND POLY-ALA-352 INS.
RX   PubMed=26005867; DOI=10.1038/ng.3308;
RA   Chen Y.C., Auer-Grumbach M., Matsukawa S., Zitzelsberger M.,
RA   Themistocleous A.C., Strom T.M., Samara C., Moore A.W., Cho L.T.,
RA   Young G.T., Weiss C., Schabhuettl M., Stucka R., Schmid A.B.,
RA   Parman Y., Graul-Neumann L., Heinritz W., Passarge E., Watson R.M.,
RA   Hertz J.M., Moog U., Baumgartner M., Valente E.M., Pereira D.,
RA   Restrepo C.M., Katona I., Dusl M., Stendel C., Wieland T.,
RA   Stafford F., Reimann F., von Au K., Finke C., Willems P.J.,
RA   Nahorski M.S., Shaikh S.S., Carvalho O.P., Nicholas A.K., Karbani G.,
RA   McAleer M.A., Cilio M.R., McHugh J.C., Murphy S.M., Irvine A.D.,
RA   Jensen U.B., Windhager R., Weis J., Bergmann C., Rautenstrauss B.,
RA   Baets J., De Jonghe P., Reilly M.M., Kropatsch R., Kurth I.,
RA   Chrast R., Michiue T., Bennett D.L., Woods C.G., Senderek J.;
RT   "Transcriptional regulator PRDM12 is essential for human pain
RT   perception.";
RL   Nat. Genet. 47:803-808(2015).
CC   -!- FUNCTION: Involved in the positive regulation of histone H3-K9
CC       dimethylation. {ECO:0000269|PubMed:26005867}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26005867}.
CC   -!- TISSUE SPECIFICITY: Not found in adult tissues except in dorsal
CC       root ganglia. {ECO:0000269|PubMed:26005867}.
CC   -!- POLYMORPHISM: The poly-alanine tract is polymorphic in the general
CC       population and contains a maximum of 14 alanines.
CC       {ECO:0000269|PubMed:26005867}.
CC   -!- DISEASE: Neuropathy, hereditary sensory and autonomic, 8 (HSAN8)
CC       [MIM:616488]: A form of hereditary sensory and autonomic
CC       neuropathy, a genetically and clinically heterogeneous group of
CC       disorders characterized by degeneration of dorsal root and
CC       autonomic ganglion cells, and by sensory and/or autonomic
CC       abnormalities. HSAN8 patients manifest congenital insensitivity to
CC       pain resulting in ulceration to the fingers, tongue, lips, and
CC       other distal appendages. Some patients may also have decreased
CC       sweating and tear production. {ECO:0000269|PubMed:26005867}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AY004252; AAG13447.2; -; mRNA.
DR   EMBL; AL359092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW87940.1; -; Genomic_DNA.
DR   CCDS; CCDS6934.1; -.
DR   RefSeq; NP_067632.2; NM_021619.2.
DR   UniGene; Hs.495311; -.
DR   PDB; 3EP0; X-ray; 2.10 A; A/B=60-229.
DR   PDBsum; 3EP0; -.
DR   ProteinModelPortal; Q9H4Q4; -.
DR   SMR; Q9H4Q4; -.
DR   STRING; 9606.ENSP00000253008; -.
DR   iPTMnet; Q9H4Q4; -.
DR   PhosphoSitePlus; Q9H4Q4; -.
DR   BioMuta; PRDM12; -.
DR   DMDM; 25008955; -.
DR   EPD; Q9H4Q4; -.
DR   PaxDb; Q9H4Q4; -.
DR   PeptideAtlas; Q9H4Q4; -.
DR   PRIDE; Q9H4Q4; -.
DR   ProteomicsDB; 80872; -.
DR   DNASU; 59335; -.
DR   Ensembl; ENST00000253008; ENSP00000253008; ENSG00000130711.
DR   GeneID; 59335; -.
DR   KEGG; hsa:59335; -.
DR   UCSC; uc004bzt.2; human.
DR   CTD; 59335; -.
DR   DisGeNET; 59335; -.
DR   EuPathDB; HostDB:ENSG00000130711.3; -.
DR   GeneCards; PRDM12; -.
DR   GeneReviews; PRDM12; -.
DR   HGNC; HGNC:13997; PRDM12.
DR   HPA; HPA043143; -.
DR   MalaCards; PRDM12; -.
DR   MIM; 616458; gene.
DR   MIM; 616488; phenotype.
DR   neXtProt; NX_Q9H4Q4; -.
DR   OpenTargets; ENSG00000130711; -.
DR   PharmGKB; PA33710; -.
DR   eggNOG; ENOG410KCSB; Eukaryota.
DR   eggNOG; ENOG410YUJ3; LUCA.
DR   GeneTree; ENSGT00940000161616; -.
DR   HOGENOM; HOG000231554; -.
DR   HOVERGEN; HBG053666; -.
DR   InParanoid; Q9H4Q4; -.
DR   OMA; TTGRMRC; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9H4Q4; -.
DR   TreeFam; TF332260; -.
DR   ChiTaRS; PRDM12; human.
DR   EvolutionaryTrace; Q9H4Q4; -.
DR   GenomeRNAi; 59335; -.
DR   PRO; PR:Q9H4Q4; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000130711; Expressed in 97 organ(s), highest expression level in vastus lateralis.
DR   Genevisible; Q9H4Q4; HS.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
DR   GO; GO:1990226; F:histone methyltransferase binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IBA:GO_Central.
DR   GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR   GO; GO:1900111; P:positive regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
DR   GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IDA:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR017126; Znf_PRDM12.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   PIRSF; PIRSF037163; PRDM12; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Disease mutation; DNA-binding;
KW   Metal-binding; Methyltransferase; Neurodegeneration; Neuropathy;
KW   Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase;
KW   Triplet repeat expansion; Zinc; Zinc-finger.
FT   CHAIN         1    367       PR domain zinc finger protein 12.
FT                                /FTId=PRO_0000047769.
FT   DOMAIN       86    203       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     243    265       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     271    293       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     299    323       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    344    359       Poly-Ala.
FT   VARIANT      31     31       D -> Y (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation; dbSNP:rs879255637).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074617.
FT   VARIANT     102    102       I -> N (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation; dbSNP:rs879255636).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074618.
FT   VARIANT     160    160       W -> C (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074619.
FT   VARIANT     168    168       R -> C (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation; dbSNP:rs767397937).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074620.
FT   VARIANT     172    172       E -> D (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation; dbSNP:rs755205487).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074621.
FT   VARIANT     289    289       H -> L (in HSAN8; no effect on nuclear
FT                                localization; not able to induce histone
FT                                H3-K9 dimethylation; dbSNP:rs879255638).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074622.
FT   VARIANT     352    352       A -> AAAAAAAA (in HSAN8; reduced protein
FT                                amount; results in protein aggregation).
FT                                {ECO:0000269|PubMed:26005867}.
FT                                /FTId=VAR_074623.
FT   STRAND       78     83       {ECO:0000244|PDB:3EP0}.
FT   STRAND       88     92       {ECO:0000244|PDB:3EP0}.
FT   STRAND       94     97       {ECO:0000244|PDB:3EP0}.
FT   STRAND       99    106       {ECO:0000244|PDB:3EP0}.
FT   STRAND      113    117       {ECO:0000244|PDB:3EP0}.
FT   STRAND      120    122       {ECO:0000244|PDB:3EP0}.
FT   STRAND      136    140       {ECO:0000244|PDB:3EP0}.
FT   STRAND      144    151       {ECO:0000244|PDB:3EP0}.
FT   HELIX       160    163       {ECO:0000244|PDB:3EP0}.
FT   TURN        170    172       {ECO:0000244|PDB:3EP0}.
FT   STRAND      175    180       {ECO:0000244|PDB:3EP0}.
FT   STRAND      183    190       {ECO:0000244|PDB:3EP0}.
FT   STRAND      199    202       {ECO:0000244|PDB:3EP0}.
SQ   SEQUENCE   367 AA;  40403 MW;  F2C665E3AE076C76 CRC64;
     MMGSVLPAEA LVLKTGLKAP GLALAEVITS DILHSFLYGR WRNVLGEQLF EDKSHHASPK
     TAFTAEVLAQ SFSGEVQKLS SLVLPAEVII AQSSIPGEGL GIFSKTWIKA GTEMGPFTGR
     VIAPEHVDIC KNNNLMWEVF NEDGTVRYFI DASQEDHRSW MTYIKCARNE QEQNLEVVQI
     GTSIFYKAIE MIPPDQELLV WYGNSHNTFL GIPGVPGLEE DQKKNKHEDF HPADSAAGPA
     GRMRCVICHR GFNSRSNLRS HMRIHTLDKP FVCRFCNRRF SQSSTLRNHV RLHTGERPYK
     CQVCQSAYSQ LAGLRAHQKS ARHRPPSTAL QAHSPALPAP HAHAPALAAA AAAAAAAAAH
     HLPAMVL
//
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