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Q13029

- PRDM2_HUMAN

UniProt

Q13029 - PRDM2_HUMAN

Protein

PR domain zinc finger protein 2

Gene

PRDM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene.1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri360 – 38223C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri390 – 41223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri483 – 50624C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1134 – 115623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1162 – 118524C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1191 – 121424C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1333 – 135523C2H2-type 7; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1455 – 147824C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    3. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Methyltransferase, 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 2 (EC:2.1.1.43)
    Alternative name(s):
    GATA-3-binding protein G3B
    Lysine N-methyltransferase 8
    MTB-ZF
    MTE-binding protein
    PR domain-containing protein 2
    Retinoblastoma protein-interacting zinc finger protein
    Zinc finger protein RIZ
    Gene namesi
    Name:PRDM2
    Synonyms:KMT8, RIZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9347. PRDM2.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061C → Y: Reduced histone methyltransferase activity. 1 Publication
    Mutagenesisi159 – 1591A → V: Reduced histone methyltransferase activity. 1 Publication
    Mutagenesisi188 – 1881I → V: Loss of histone methyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33715.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17181718PR domain zinc finger protein 2PRO_0000041634Add
    BLAST

    Proteomic databases

    MaxQBiQ13029.
    PaxDbiQ13029.
    PRIDEiQ13029.

    PTM databases

    PhosphoSiteiQ13029.

    Expressioni

    Tissue specificityi

    Highly expressed in retinoblastoma cell lines and in brain tumors. Also expressed in a number of other cell lines and in brain, heart, skeletal muscle, liver and spleen. Isoform 1 is expressed in testis at much higher level than isoform 3.2 Publications

    Gene expression databases

    ArrayExpressiQ13029.
    BgeeiQ13029.
    CleanExiHS_PRDM2.
    GenevestigatoriQ13029.

    Organism-specific databases

    HPAiHPA005809.

    Interactioni

    Subunit structurei

    Binds to the retinoblastoma protein (RB). Interacts with GATA3.2 Publications

    Protein-protein interaction databases

    BioGridi113575. 8 interactions.
    DIPiDIP-428N.
    IntActiQ13029. 2 interactions.
    STRINGi9606.ENSP00000235372.

    Structurei

    Secondary structure

    1
    1718
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Helixi15 – 173
    Helixi20 – 245
    Beta strandi27 – 293
    Beta strandi30 – 345
    Turni36 – 394
    Beta strandi41 – 488
    Beta strandi54 – 596
    Beta strandi62 – 643
    Helixi66 – 683
    Beta strandi72 – 809
    Turni81 – 833
    Beta strandi84 – 896
    Helixi93 – 953
    Helixi98 – 1014
    Beta strandi106 – 1105
    Beta strandi113 – 1186
    Beta strandi121 – 1288
    Helixi146 – 15813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JV0NMR-A1-161[»]
    2QPWX-ray1.79A2-148[»]
    ProteinModelPortaliQ13029.
    SMRiQ13029. Positions 2-148, 386-412, 1131-1210, 1266-1298, 1328-1353, 1444-1485.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13029.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 141114SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni294 – 31623Retinoblastoma protein bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi970 – 97910SH3-bindingSequence Analysis
    Motifi985 – 99814SH3-bindingSequence AnalysisAdd
    BLAST
    Motifi1028 – 105225SH3-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi268 – 29629Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi933 – 1049117Pro-richAdd
    BLAST
    Compositional biasi1052 – 107423Poly-SerAdd
    BLAST
    Compositional biasi1361 – 144787Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 8 C2H2-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri360 – 38223C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri390 – 41223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri483 – 50624C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1134 – 115623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1162 – 118524C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1191 – 121424C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1333 – 135523C2H2-type 7; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1455 – 147824C2H2-type 8; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG258873.
    HOGENOMiHOG000231078.
    HOVERGENiHBG053671.
    InParanoidiQ13029.
    KOiK11432.
    OMAiTHTNMRR.
    OrthoDBiEOG7NW68B.
    PhylomeDBiQ13029.
    TreeFamiTF332173.

    Family and domain databases

    Gene3Di3.30.160.60. 1 hit.
    InterProiIPR009170. RIZ_retinblastoma-bd_prot.
    IPR001214. SET_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002395. RIZ_SET. 1 hit.
    SMARTiSM00317. SET. 1 hit.
    SM00355. ZnF_C2H2. 8 hits.
    [Graphical view]
    PROSITEiPS50280. SET. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 6 hits.
    PS50157. ZINC_FINGER_C2H2_2. 7 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q13029-1) [UniParc]FASTAAdd to Basket

    Also known as: RIZ1

    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

    MNQNTTEPVA ATETLAEVPE HVLRGLPEEV RLFPSAVDKT RIGVWATKPI     50
    LKGKKFGPFV GDKKKRSQVK NNVYMWEVYY PNLGWMCIDA TDPEKGNWLR 100
    YVNWACSGEE QNLFPLEINR AIYYKTLKPI APGEELLVWY NGEDNPEIAA 150
    AIEEERASAR SKRSSPKSRK GKKKSQENKN KGNKIQDIQL KTSEPDFTSA 200
    NMRDSAEGPK EDEEKPSASA LEQPATLQEV ASQEVPPELA TPAPAWEPQP 250
    EPDERLEAAA CEVNDLGEEE EEEEEEDEEE EEDDDDDELE DEGEEEASMP 300
    NENSVKEPEI RCDEKPEDLL EEPKTTSEET LEDCSEVTPA MQIPRTKEEA 350
    NGDVFETFMF PCQHCERKFT TKQGLERHMH IHISTVNHAF KCKYCGKAFG 400
    TQINRRRHER RHEAGLKRKP SQTLQPSEDL ADGKASGENV ASKDDSSPPS 450
    LGPDCLIMNS EKASQDTINS SVVEENGEVK ELHPCKYCKK VFGTHTNMRR 500
    HQRRVHERHL IPKGVRRKGG LEEPQPPAEQ AQATQNVYVP STEPEEEGEA 550
    DDVYIMDISS NISENLNYYI DGKIQTNNNT SNCDVIEMES ASADLYGINC 600
    LLTPVTVEIT QNIKTTQVPV TEDLPKEPLG STNSEAKKRR TASPPALPKI 650
    KAETDSDPMV PSCSLSLPLS ISTTEAVSFH KEKSVYLSSK LKQLLQTQDK 700
    LTPAGISATE IAKLGPVCVS APASMLPVTS SRFKRRTSSP PSSPQHSPAL 750
    RDFGKPSDGK AAWTDAGLTS KKSKLESHSD SPAWSLSGRD ERETVSPPCF 800
    DEYKMSKEWT ASSAFSSVCN QQPLDLSSGV KQKAEGTGKT PVQWESVLDL 850
    SVHKKHCSDS EGKEFKESHS VQPTCSAVKK RKPTTCMLQK VLLNEYNGID 900
    LPVENPADGT RSPSPCKSLE AQPDPDLGPG SGFPAPTVES TPDVCPSSPA 950
    LQTPSLSSGQ LPPLLIPTDP SSPPPCPPVL TVATPPPPLL PTVPLPAPSS 1000
    SASPHPCPSP LSNATAQSPL PILSPTVSPS PSPIPPVEPL MSAASPGPPT 1050
    LSSSSSSSSS SSSFSSSSSS SSPSPPPLSA ISSVVSSGDN LEASLPMISF 1100
    KQEELENEGL KPREEPQSAA EQDVVVQETF NKNFVCNVCE SPFLSIKDLT 1150
    KHLSIHAEEW PFKCEFCVQL FKDKTDLSEH RFLLHGVGNI FVCSVCKKEF 1200
    AFLCNLQQHQ RDLHPDKVCT HHEFESGTLR PQNFTDPSKA HVEHMQSLPE 1250
    DPLETSKEEE ELNDSSEELY TTIKIMASGI KTKDPDVRLG LNQHYPSFKP 1300
    PPFQYHHRNP MGIGVTATNF TTHNIPQTFT TAIRCTKCGK GVDNMPELHK 1350
    HILACASASD KKRYTPKKNP VPLKQTVQPK NGVVVLDNSG KNAFRRMGQP 1400
    KRLNFSVELS KMSSNKLKLN ALKKKNQLVQ KAILQKNKSA KQKADLKNAC 1450
    ESSSHICPYC NREFTYIGSL NKHAAFSCPK KPLSPPKKKV SHSSKKGGHS 1500
    SPASSDKNSN SNHRRRTADA EIKMQSMQTP LGKTRARSSG PTQVPLPSSS 1550
    FRSKQNVKFA ASVKSKKPSS SSLRNSSPIR MAKITHVEGK KPKAVAKNHS 1600
    AQLSSKTSRS LHVRVQKSKA VLQSKSTLAS KKRTDRFNIK SRERSGGPVT 1650
    RSLQLAAAAD LSENKREDGS AKQELKDFSY SLRLASRCSP PAAPYITRQY 1700
    RKVKAPAAAQ FQGPFFKE 1718
    Length:1,718
    Mass (Da):188,915
    Last modified:December 21, 2004 - v3
    Checksum:i536BD68667AFE433
    GO
    Isoform 2 (identifier: Q13029-2) [UniParc]FASTAAdd to Basket

    Also known as: MTB-Zf

    The sequence of this isoform differs from the canonical sequence as follows:
         1679-1682: SYSL → RNFL
         1683-1718: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,682
    Mass (Da):184,961
    Checksum:iF353A6402F93712D
    GO
    Isoform 3 (identifier: Q13029-3) [UniParc]FASTAAdd to Basket

    Also known as: RIZ2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-201: Missing.

    Note: Produced by alternative initiation at Met-202 of isoform 1.

    Show »
    Length:1,517
    Mass (Da):166,061
    Checksum:i2AB9A94179532CE7
    GO
    Isoform 4 (identifier: Q13029-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         171-226: GKKKSQENKN...SASALEQPAT → ATASAWRPDA...LTAPEVTWNQ
         227-1718: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:226
    Mass (Da):25,519
    Checksum:iD7CE11A6D48E16D7
    GO
    Isoform 5 (identifier: Q13029-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-201: Missing.
         1679-1682: SYSL → RNFL
         1683-1718: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,481
    Mass (Da):162,107
    Checksum:i87F7398540D3A5F3
    GO

    Sequence cautioni

    The sequence BAA08110.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641S → T in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti196 – 1961D → S in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti200 – 2001A → G in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti276 – 29318EDEEE…LEDEG → VGGGGGVVVVVSWKARGE in AAA87023. (PubMed:7590293)CuratedAdd
    BLAST
    Sequence conflicti307 – 31812EPEIR…EKPED → SQKYGVMRSQKI in AAA87023. (PubMed:7590293)CuratedAdd
    BLAST
    Sequence conflicti336 – 3372EV → DL in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti371 – 3711T → I in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti466 – 4672DT → VS in AAA87023. (PubMed:7590293)Curated
    Sequence conflicti530 – 5301Q → L in BX647310. (PubMed:17974005)Curated
    Sequence conflicti534 – 55017TQNVY…EEGEA → PRTCMYQAQSRRGRGSR in AAA87023. (PubMed:7590293)CuratedAdd
    BLAST
    Sequence conflicti703 – 7031P → PP(PubMed:7538672)Curated
    Sequence conflicti703 – 7031P → PP(PubMed:8654390)Curated
    Sequence conflicti856 – 8561H → R in BX647310. (PubMed:17974005)Curated
    Sequence conflicti1456 – 14561I → T in BX647310. (PubMed:17974005)Curated
    Isoform 4 (identifier: Q13029-4)
    Sequence conflicti198 – 1981Q → R in BC014468. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti283 – 2831D → E.
    Corresponds to variant rs2076324 [ dbSNP | Ensembl ].
    VAR_052929
    Natural varianti450 – 4501S → N.
    Corresponds to variant rs17350795 [ dbSNP | Ensembl ].
    VAR_052930

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 201201Missing in isoform 3 and isoform 5. 1 PublicationVSP_018974Add
    BLAST
    Alternative sequencei171 – 22656GKKKS…EQPAT → ATASAWRPDALHQRPRTSPG SIGRSKLQLQPSSRDHSSKS RHSGCSLTAPEVTWNQ in isoform 4. 1 PublicationVSP_046421Add
    BLAST
    Alternative sequencei227 – 17181492Missing in isoform 4. 1 PublicationVSP_046422Add
    BLAST
    Alternative sequencei1679 – 16824SYSL → RNFL in isoform 2 and isoform 5. 2 PublicationsVSP_006927
    Alternative sequencei1683 – 171836Missing in isoform 2 and isoform 5. 2 PublicationsVSP_006928Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17838 mRNA. Translation: AAC50820.2.
    BX647310 mRNA. No translation available.
    AL031277, AL583942 Genomic DNA. Translation: CAI19343.1.
    AL583942, AL031277 Genomic DNA. Translation: CAH70943.1.
    AL359771 Genomic DNA. No translation available.
    BC014468 mRNA. No translation available.
    U23736 mRNA. Translation: AAA87023.1.
    D45132 mRNA. Translation: BAA08110.1. Different initiation.
    CCDSiCCDS150.1. [Q13029-1]
    CCDS151.1. [Q13029-2]
    CCDS30603.1. [Q13029-5]
    CCDS44061.1. [Q13029-4]
    PIRiI38902.
    RefSeqiNP_001007258.1. NM_001007257.2. [Q13029-5]
    NP_001129082.1. NM_001135610.1. [Q13029-4]
    NP_036363.2. NM_012231.4. [Q13029-1]
    NP_056950.2. NM_015866.4. [Q13029-2]
    XP_005246050.1. XM_005245993.1. [Q13029-1]
    XP_005246054.1. XM_005245997.1. [Q13029-3]
    XP_005246055.1. XM_005245998.1. [Q13029-5]
    XP_006710940.1. XM_006710877.1. [Q13029-2]
    XP_006710941.1. XM_006710878.1. [Q13029-3]
    XP_006710942.1. XM_006710879.1. [Q13029-3]
    XP_006710943.1. XM_006710880.1. [Q13029-3]
    UniGeneiHs.371823.

    Genome annotation databases

    EnsembliENST00000235372; ENSP00000235372; ENSG00000116731. [Q13029-1]
    ENST00000311066; ENSP00000312352; ENSG00000116731. [Q13029-2]
    ENST00000343137; ENSP00000341621; ENSG00000116731. [Q13029-5]
    ENST00000376048; ENSP00000365216; ENSG00000116731. [Q13029-4]
    ENST00000413440; ENSP00000411103; ENSG00000116731. [Q13029-5]
    GeneIDi7799.
    KEGGihsa:7799.
    UCSCiuc001avh.3. human. [Q13029-2]
    uc001avi.3. human. [Q13029-1]

    Polymorphism databases

    DMDMi56757653.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17838 mRNA. Translation: AAC50820.2 .
    BX647310 mRNA. No translation available.
    AL031277 , AL583942 Genomic DNA. Translation: CAI19343.1 .
    AL583942 , AL031277 Genomic DNA. Translation: CAH70943.1 .
    AL359771 Genomic DNA. No translation available.
    BC014468 mRNA. No translation available.
    U23736 mRNA. Translation: AAA87023.1 .
    D45132 mRNA. Translation: BAA08110.1 . Different initiation.
    CCDSi CCDS150.1. [Q13029-1 ]
    CCDS151.1. [Q13029-2 ]
    CCDS30603.1. [Q13029-5 ]
    CCDS44061.1. [Q13029-4 ]
    PIRi I38902.
    RefSeqi NP_001007258.1. NM_001007257.2. [Q13029-5 ]
    NP_001129082.1. NM_001135610.1. [Q13029-4 ]
    NP_036363.2. NM_012231.4. [Q13029-1 ]
    NP_056950.2. NM_015866.4. [Q13029-2 ]
    XP_005246050.1. XM_005245993.1. [Q13029-1 ]
    XP_005246054.1. XM_005245997.1. [Q13029-3 ]
    XP_005246055.1. XM_005245998.1. [Q13029-5 ]
    XP_006710940.1. XM_006710877.1. [Q13029-2 ]
    XP_006710941.1. XM_006710878.1. [Q13029-3 ]
    XP_006710942.1. XM_006710879.1. [Q13029-3 ]
    XP_006710943.1. XM_006710880.1. [Q13029-3 ]
    UniGenei Hs.371823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JV0 NMR - A 1-161 [» ]
    2QPW X-ray 1.79 A 2-148 [» ]
    ProteinModelPortali Q13029.
    SMRi Q13029. Positions 2-148, 386-412, 1131-1210, 1266-1298, 1328-1353, 1444-1485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113575. 8 interactions.
    DIPi DIP-428N.
    IntActi Q13029. 2 interactions.
    STRINGi 9606.ENSP00000235372.

    PTM databases

    PhosphoSitei Q13029.

    Polymorphism databases

    DMDMi 56757653.

    Proteomic databases

    MaxQBi Q13029.
    PaxDbi Q13029.
    PRIDEi Q13029.

    Protocols and materials databases

    DNASUi 7799.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000235372 ; ENSP00000235372 ; ENSG00000116731 . [Q13029-1 ]
    ENST00000311066 ; ENSP00000312352 ; ENSG00000116731 . [Q13029-2 ]
    ENST00000343137 ; ENSP00000341621 ; ENSG00000116731 . [Q13029-5 ]
    ENST00000376048 ; ENSP00000365216 ; ENSG00000116731 . [Q13029-4 ]
    ENST00000413440 ; ENSP00000411103 ; ENSG00000116731 . [Q13029-5 ]
    GeneIDi 7799.
    KEGGi hsa:7799.
    UCSCi uc001avh.3. human. [Q13029-2 ]
    uc001avi.3. human. [Q13029-1 ]

    Organism-specific databases

    CTDi 7799.
    GeneCardsi GC01P014026.
    HGNCi HGNC:9347. PRDM2.
    HPAi HPA005809.
    MIMi 601196. gene.
    neXtProti NX_Q13029.
    PharmGKBi PA33715.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258873.
    HOGENOMi HOG000231078.
    HOVERGENi HBG053671.
    InParanoidi Q13029.
    KOi K11432.
    OMAi THTNMRR.
    OrthoDBi EOG7NW68B.
    PhylomeDBi Q13029.
    TreeFami TF332173.

    Miscellaneous databases

    EvolutionaryTracei Q13029.
    GeneWikii PRDM2.
    GenomeRNAii 7799.
    NextBioi 30170.
    PROi Q13029.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13029.
    Bgeei Q13029.
    CleanExi HS_PRDM2.
    Genevestigatori Q13029.

    Family and domain databases

    Gene3Di 3.30.160.60. 1 hit.
    InterProi IPR009170. RIZ_retinblastoma-bd_prot.
    IPR001214. SET_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002395. RIZ_SET. 1 hit.
    SMARTi SM00317. SET. 1 hit.
    SM00355. ZnF_C2H2. 8 hits.
    [Graphical view ]
    PROSITEi PS50280. SET. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 6 hits.
    PS50157. ZINC_FINGER_C2H2_2. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein."
      Buyse I.M., Shao G., Huang S.
      Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Fetal brain and Retinoblastoma.
    2. "The retinoblastoma interacting zinc finger gene RIZ produces a PR domain-lacking product through an internal promoter."
      Liu L., Shao G., Steele-Perkins G., Huang S.
      J. Biol. Chem. 272:2984-2991(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3), ALTERNATIVE INITIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Retina.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 4).
    6. "Identification and cloning of the G3B cDNA encoding a 3' segment of a protein binding to GATA-3."
      Shapiro V.S., Lee P., Winoto A.
      Gene 163:329-330(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 159-550, INTERACTION WITH GATA3.
    7. "cDNA cloning of a novel protein containing two zinc-finger domains that may function as a transcription factor for the human heme-oxygenase-1 gene."
      Muraosa Y., Takahashi K., Yoshizawa M., Shibahara S.
      Eur. J. Biochem. 235:471-479(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-1718 (ISOFORM 2), TISSUE SPECIFICITY.
    8. "Inactivation of a histone methyltransferase by mutations in human cancers."
      Kim K.-C., Geng L., Huang S.
      Cancer Res. 63:7619-7623(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-106; ALA-159 AND ILE-188, SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: STRUCTURE BY NMR OF 1-161, INTERACTION WITH HISTONE H3.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 2-148.

    Entry informationi

    Entry nameiPRDM2_HUMAN
    AccessioniPrimary (citable) accession number: Q13029
    Secondary accession number(s): B1AJZ4
    , B5MC68, Q13149, Q14550, Q5THJ1, Q5VUL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3