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Q9NQX1

- PRDM5_HUMAN

UniProt

Q9NQX1 - PRDM5_HUMAN

Protein

PR domain zinc finger protein 5

Gene

PRDM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    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. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May caused G2/M arrest and apoptosis in cancer cells.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri167 – 19024C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri199 – 22123C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri234 – 25623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri262 – 28726C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri295 – 31723C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri320 – 34223C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri348 – 37023C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri376 – 39823C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri404 – 42623C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri432 – 45524C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri461 – 48323C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri489 – 51123C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri517 – 53923C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri545 – 56723C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri573 – 59523C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri602 – 62524C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. methyltransferase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. repressing transcription factor binding Source: UniProtKB
    5. sequence-specific DNA binding Source: UniProtKB
    6. transcription regulatory region DNA binding Source: UniProtKB
    7. transcription regulatory region sequence-specific DNA binding Source: InterPro

    GO - Biological processi

    1. histone deacetylation Source: UniProtKB
    2. histone H3-K9 methylation Source: UniProtKB
    3. mitotic cell cycle Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PR domain zinc finger protein 5 (EC:2.1.1.-)
    Alternative name(s):
    PR domain-containing protein 5
    Gene namesi
    Name:PRDM5
    Synonyms:PFM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9349. PRDM5.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Brittle cornea syndrome 2 (BCS2) [MIM:614170]: A disorder characterized by extreme corneal thinning resulting in corneal rupture after minor trauma, blue sclerae, keratoconus or keratoglobus, hyperelasticity of the skin, and hypermobile joints.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071Y → C in BCS2. 1 Publication
    VAR_066393

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614170. phenotype.
    Orphaneti90354. Brittle cornea syndrome.
    PharmGKBiPA33717.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 630630PR domain zinc finger protein 5PRO_0000047761Add
    BLAST

    Proteomic databases

    PaxDbiQ9NQX1.
    PRIDEiQ9NQX1.

    PTM databases

    PhosphoSiteiQ9NQX1.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in colon and ovary. Tends to be silenced in breast, colorectal, gastric and liver cancer tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9NQX1.
    BgeeiQ9NQX1.
    CleanExiHS_PRDM5.
    GenevestigatoriQ9NQX1.

    Organism-specific databases

    HPAiHPA051406.

    Interactioni

    Subunit structurei

    Interacts with EHMT2/G9A, GFI1 and HDAC1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EHMT2Q96KQ73EBI-4292031,EBI-744366
    GFI1Q996842EBI-4292031,EBI-949368
    HDAC1Q135473EBI-4292031,EBI-301834

    Protein-protein interaction databases

    BioGridi116287. 3 interactions.
    IntActiQ9NQX1. 3 interactions.
    STRINGi9606.ENSP00000264808.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NQX1.
    SMRiQ9NQX1. Positions 4-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 124117SETPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 16 C2H2-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri167 – 19024C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri199 – 22123C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri234 – 25623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri262 – 28726C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri295 – 31723C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri320 – 34223C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri348 – 37023C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri376 – 39823C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri404 – 42623C2H2-type 9PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri432 – 45524C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri461 – 48323C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri489 – 51123C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri517 – 53923C2H2-type 13PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri545 – 56723C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri573 – 59523C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri602 – 62524C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000234617.
    HOVERGENiHBG098380.
    InParanoidiQ9NQX1.
    OMAiLGCKEDY.
    OrthoDBiEOG7KSX7Q.
    PhylomeDBiQ9NQX1.
    TreeFamiTF106478.

    Family and domain databases

    Gene3Di3.30.160.60. 14 hits.
    InterProiIPR001214. SET_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    IPR022755. Znf_C2H2_jaz.
    IPR017125. Znf_PRDM5.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 3 hits.
    PF12171. zf-C2H2_jaz. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037162. PRDM. 1 hit.
    SMARTiSM00317. SET. 1 hit.
    SM00355. ZnF_C2H2. 16 hits.
    [Graphical view]
    PROSITEiPS50280. SET. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 14 hits.
    PS50157. ZINC_FINGER_C2H2_2. 16 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQX1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLGMYVPDRF SLKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE    50
    NMDYRLMWEV RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QEQKNLAAIQ 100
    EGENIFYLAV EDIETDTELL IGYLDSDMEA EEEEQQIMTV IKEGEVENSR 150
    RQSTAGRKDR LGCKEDYACP QCESSFTSED ILAEHLQTLH QKPTEEKEFK 200
    CKNCGKKFPV KQALQRHVLQ CTAKSSLKES SRSFQCSVCN SSFSSASSFE 250
    QHQETCRGDA RFVCKADSCG KRLKSKDALK RHQENVHTGD PKKKLICSVC 300
    NKKCSSASSL QEHRKIHEIF DCQECMKKFI SANQLKRHMI THSEKRPYNC 350
    EICNKSFKRL DQVGAHKVIH SEDKPYKCKL CGKGFAHRNV YKNHKKTHSE 400
    ERPFQCEECK ALFRTPFSLQ RHLLIHNSER TFKCHHCDAT FKRKDTLNVH 450
    VQVVHERHKK YRCELCNKAF VTPSVLRSHK KTHTGEKEKI CPYCGQKFAS 500
    SGTLRVHIRS HTGERPYQCP YCEKGFSKND GLKMHIRTHT REKPYKCSEC 550
    SKAFSQKRGL DEHKRTHTGE KPFQCDVCDL AFSLKKMLIR HKMTHNPNRP 600
    LAECQFCHKK FTRNDYLKVH MDNIHGVADS 630
    Length:630
    Mass (Da):73,090
    Last modified:November 4, 2008 - v2
    Checksum:iD16AF81AB5A34398
    GO
    Isoform 2 (identifier: Q9NQX1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         218-248: Missing.

    Show »
    Length:599
    Mass (Da):69,862
    Checksum:i567E937469373B58
    GO
    Isoform 3 (identifier: Q9NQX1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-111: EGENIFYLAVE → DKNLGPAEWRG
         112-630: Missing.

    Show »
    Length:111
    Mass (Da):12,874
    Checksum:iF0568A1C8495EC01
    GO
    Isoform 4 (identifier: Q9NQX1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         218-248: Missing.
         515-532: RPYQCPYCEKGFSKNDGL → AVQVLRVQQGLQPEARPG
         533-630: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:501
    Mass (Da):58,124
    Checksum:i5560F041B4F4B3E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611R → K in AAF78077. (PubMed:15077163)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071Y → C in BCS2. 1 Publication
    VAR_066393

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei101 – 11111EGENIFYLAVE → DKNLGPAEWRG in isoform 3. 2 PublicationsVSP_035652Add
    BLAST
    Alternative sequencei112 – 630519Missing in isoform 3. 2 PublicationsVSP_035653Add
    BLAST
    Alternative sequencei218 – 24831Missing in isoform 2 and isoform 4. 1 PublicationVSP_035654Add
    BLAST
    Alternative sequencei515 – 53218RPYQC…KNDGL → AVQVLRVQQGLQPEARPG in isoform 4. 1 PublicationVSP_054395Add
    BLAST
    Alternative sequencei533 – 63098Missing in isoform 4. 1 PublicationVSP_054396Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272897 mRNA. Translation: AAF78077.1.
    AK056352 mRNA. Translation: BAG51686.1.
    AC025741 Genomic DNA. No translation available.
    AC104068 Genomic DNA. No translation available.
    AC104795 Genomic DNA. No translation available.
    BC066942 mRNA. Translation: AAH66942.1.
    BC121037 mRNA. Translation: AAI21038.1.
    BC121038 mRNA. Translation: AAI21039.1.
    CCDSiCCDS3716.1. [Q9NQX1-1]
    RefSeqiNP_061169.2. NM_018699.2. [Q9NQX1-1]
    XP_005262763.1. XM_005262706.1. [Q9NQX1-2]
    XP_005262764.1. XM_005262707.1. [Q9NQX1-4]
    UniGeneiHs.666782.
    Hs.669312.

    Genome annotation databases

    EnsembliENST00000264808; ENSP00000264808; ENSG00000138738. [Q9NQX1-1]
    ENST00000394435; ENSP00000377955; ENSG00000138738. [Q9NQX1-3]
    ENST00000428209; ENSP00000404832; ENSG00000138738. [Q9NQX1-2]
    ENST00000515109; ENSP00000422309; ENSG00000138738. [Q9NQX1-4]
    GeneIDi11107.
    KEGGihsa:11107.
    UCSCiuc003idn.3. human. [Q9NQX1-1]
    uc003ido.3. human. [Q9NQX1-2]
    uc003idp.1. human. [Q9NQX1-3]

    Polymorphism databases

    DMDMi212276458.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF272897 mRNA. Translation: AAF78077.1 .
    AK056352 mRNA. Translation: BAG51686.1 .
    AC025741 Genomic DNA. No translation available.
    AC104068 Genomic DNA. No translation available.
    AC104795 Genomic DNA. No translation available.
    BC066942 mRNA. Translation: AAH66942.1 .
    BC121037 mRNA. Translation: AAI21038.1 .
    BC121038 mRNA. Translation: AAI21039.1 .
    CCDSi CCDS3716.1. [Q9NQX1-1 ]
    RefSeqi NP_061169.2. NM_018699.2. [Q9NQX1-1 ]
    XP_005262763.1. XM_005262706.1. [Q9NQX1-2 ]
    XP_005262764.1. XM_005262707.1. [Q9NQX1-4 ]
    UniGenei Hs.666782.
    Hs.669312.

    3D structure databases

    ProteinModelPortali Q9NQX1.
    SMRi Q9NQX1. Positions 4-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116287. 3 interactions.
    IntActi Q9NQX1. 3 interactions.
    STRINGi 9606.ENSP00000264808.

    PTM databases

    PhosphoSitei Q9NQX1.

    Polymorphism databases

    DMDMi 212276458.

    Proteomic databases

    PaxDbi Q9NQX1.
    PRIDEi Q9NQX1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264808 ; ENSP00000264808 ; ENSG00000138738 . [Q9NQX1-1 ]
    ENST00000394435 ; ENSP00000377955 ; ENSG00000138738 . [Q9NQX1-3 ]
    ENST00000428209 ; ENSP00000404832 ; ENSG00000138738 . [Q9NQX1-2 ]
    ENST00000515109 ; ENSP00000422309 ; ENSG00000138738 . [Q9NQX1-4 ]
    GeneIDi 11107.
    KEGGi hsa:11107.
    UCSCi uc003idn.3. human. [Q9NQX1-1 ]
    uc003ido.3. human. [Q9NQX1-2 ]
    uc003idp.1. human. [Q9NQX1-3 ]

    Organism-specific databases

    CTDi 11107.
    GeneCardsi GC04M121613.
    HGNCi HGNC:9349. PRDM5.
    HPAi HPA051406.
    MIMi 614161. gene.
    614170. phenotype.
    neXtProti NX_Q9NQX1.
    Orphaneti 90354. Brittle cornea syndrome.
    PharmGKBi PA33717.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000234617.
    HOVERGENi HBG098380.
    InParanoidi Q9NQX1.
    OMAi LGCKEDY.
    OrthoDBi EOG7KSX7Q.
    PhylomeDBi Q9NQX1.
    TreeFami TF106478.

    Miscellaneous databases

    GenomeRNAii 11107.
    NextBioi 42230.
    PROi Q9NQX1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQX1.
    Bgeei Q9NQX1.
    CleanExi HS_PRDM5.
    Genevestigatori Q9NQX1.

    Family and domain databases

    Gene3Di 3.30.160.60. 14 hits.
    InterProi IPR001214. SET_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    IPR022755. Znf_C2H2_jaz.
    IPR017125. Znf_PRDM5.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 3 hits.
    PF12171. zf-C2H2_jaz. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037162. PRDM. 1 hit.
    SMARTi SM00317. SET. 1 hit.
    SM00355. ZnF_C2H2. 16 hits.
    [Graphical view ]
    PROSITEi PS50280. SET. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 14 hits.
    PS50157. ZINC_FINGER_C2H2_2. 16 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PRDM5 is silenced in human cancers and has growth suppressive activities."
      Deng Q., Huang S.
      Oncogene 23:4903-4910(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 2; 3 AND 4).
      Tissue: Brain.
    5. Cited for: TISSUE SPECIFICITY.
    6. "Epigenetic regulation of protein-coding and microRNA genes by the Gfi1-interacting tumor suppressor PRDM5."
      Duan Z., Person R.E., Lee H.-H., Huang S., Donadieu J., Badolato R., Grimes H.L., Papayannopoulou T., Horwitz M.S.
      Mol. Cell. Biol. 27:6889-6902(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EHMT2; GFI1 AND HDAC1, SUBCELLULAR LOCATION.
    7. Cited for: VARIANT BCS2 CYS-107, FUNCTION.

    Entry informationi

    Entry nameiPRDM5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQX1
    Secondary accession number(s): Q0VAI9, Q0VAJ0, Q6NXQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3