Reviewed,
UniProtKB/Swiss-Prot Q13029 (PRDM2_HUMAN)
Last modified
November 25, 2008.
Version 88.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: PR domain zinc finger protein 2 Alternative name(s): PR domain-containing protein 2 Retinoblastoma protein-interacting zinc finger protein Zinc finger protein RIZ MTE-binding protein MTB-ZF GATA-3-binding protein G3B Lysine N-methyltransferase 8 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1718 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. |
| Subunit structure | Binds to the retinoblastoma protein (RB). Interacts with GATA3. |
| Subcellular location | |
| Tissue specificity | 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. |
| Sequence similarities | Contains 8 C2H2-type zinc fingers. Contains 1 SET domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative initiation Alternative splicing |
| Domain | Repeat Zinc-finger |
| Ligand | DNA-binding Metal-binding Zinc |
| Molecular function | Activator |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Ref.4 Ref.5 Non-traceable author statement. Source: UniProtKB |
| Cellular component | Golgi apparatus Inferred from direct assay. Source: HPA nucleus Ref.1 Ref.4Non-traceable author statement. Source: UniProtKB |
| Molecular function | transcription factor activity Ref.4 Ref.5 Non-traceable author statement. Source: UniProtKB zinc ion binding Ref.1Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q13029-1) 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. | ||||||
| Isoform 2 (identifier: Q13029-2) Also known as: MTB-Zf; The sequence of this isoform differs from the canonical sequence as follows: 1679-1682: SYSL → RNFL 1683-1718: Missing. | ||||||
| Notes: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: Q13029-3) Also known as: RIZ2; The sequence of this isoform differs from the canonical sequence as follows: 1-201: Missing. | ||||||
| Notes: Produced by alternative initiation at Met-202 of isoform 1. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1718 | 1718 | PR domain zinc finger protein 2 | PRO_0000041634 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Domain | 27 – 145 | 119 | SET | ||||||||||||||||||||||||||||||||||
| Zinc finger | 360 – 382 | 23 | C2H2-type 1 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 390 – 412 | 23 | C2H2-type 2 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 483 – 506 | 24 | C2H2-type 3 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 1134 – 1156 | 23 | C2H2-type 4 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 1162 – 1185 | 24 | C2H2-type 5 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 1191 – 1214 | 24 | C2H2-type 6 | ||||||||||||||||||||||||||||||||||
| Zinc finger | 1333 – 1355 | 23 | C2H2-type 7; atypical | ||||||||||||||||||||||||||||||||||
| Zinc finger | 1455 – 1478 | 24 | C2H2-type 8; atypical | ||||||||||||||||||||||||||||||||||
| Region | 294 – 316 | 23 | Retinoblastoma protein binding | ||||||||||||||||||||||||||||||||||
| Motif | 970 – 979 | 10 | SH3-binding Potential | ||||||||||||||||||||||||||||||||||
| Motif | 985 – 998 | 14 | SH3-binding Potential | ||||||||||||||||||||||||||||||||||
| Motif | 1028 – 1052 | 25 | SH3-binding Potential | ||||||||||||||||||||||||||||||||||
| Compositional bias | 268 – 296 | 29 | Asp/Glu-rich (acidic) | ||||||||||||||||||||||||||||||||||
| Compositional bias | 933 – 1049 | 117 | Pro-rich | ||||||||||||||||||||||||||||||||||
| Compositional bias | 1052 – 1074 | 23 | Poly-Ser | ||||||||||||||||||||||||||||||||||
| Compositional bias | 1361 – 1447 | 87 | Arg/Lys-rich (basic) | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 641 | 1 | Phosphothreonine | ||||||||||||||||||||||||||||||||||
| Modified residue | 643 | 1 | Phosphoserine | ||||||||||||||||||||||||||||||||||
| Modified residue | 739 | 1 | Phosphoserine | ||||||||||||||||||||||||||||||||||
| Modified residue | 743 | 1 | Phosphoserine | ||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 201 | 201 | Missing in isoform 3. | VSP_018974 | |||||||||||||||||||||||||||||||||
| Alternative sequence | 1679 – 1682 | 4 | SYSL → RNFL in isoform 2. | VSP_006927 | |||||||||||||||||||||||||||||||||
| Alternative sequence | 1683 – 1718 | 36 | Missing in isoform 2. | VSP_006928 | |||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 164 | 1 | S → T in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 196 | 1 | D → S in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 200 | 1 | A → G in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 276 – 293 | 18 | EDEEE…LEDEG → VGGGGGVVVVVSWKARGE in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 307 – 318 | 12 | EPEIR…EKPED → SQKYGVMRSQKI in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 336 – 337 | 2 | EV → DL in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 371 | 1 | T → I in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 466 – 467 | 2 | DT → VS in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 534 – 550 | 17 | TQNVY…EEGEA → PRTCMYQAQSRRGRGSR in AAA87023. Ref.4 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 703 | 1 | P → PP Ref.1 Ref.5 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 7 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 15 – 17 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 20 – 24 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 30 – 34 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 41 – 48 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 62 – 64 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 66 – 68 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 72 – 80 | 9 | |||||||||||||||||||||||||||||||||||
| Turn | 81 – 83 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 89 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 93 – 95 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 98 – 101 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 118 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 121 – 128 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 149 – 158 | 10 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 7538672] [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: 9006946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3), ALTERNATIVE INITIATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [3] | "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. |

Clusters with