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Q13029

- PRDM2_HUMAN

UniProt

Q13029 - PRDM2_HUMAN

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Protein
PR domain zinc finger protein 2
Gene
PRDM2, KMT8, RIZ
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1
Add
BLAST
Zinc fingeri390 – 41223C2H2-type 2
Add
BLAST
Zinc fingeri483 – 50624C2H2-type 3
Add
BLAST
Zinc fingeri1134 – 115623C2H2-type 4
Add
BLAST
Zinc fingeri1162 – 118524C2H2-type 5
Add
BLAST
Zinc fingeri1191 – 121424C2H2-type 6
Add
BLAST
Zinc fingeri1333 – 135523C2H2-type 7; atypical
Add
BLAST
Zinc fingeri1455 – 147824C2H2-type 8; atypical
Add
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
Complete GO annotation...

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
Complete GO annotation...

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 2
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ13029.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 141114SET
Add
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi970 – 97910SH3-binding Reviewed prediction
Motifi985 – 99814SH3-binding Reviewed prediction
Add
BLAST
Motifi1028 – 105225SH3-binding Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 SET domain.

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.

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.

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.
VSP_018974Add
BLAST
Alternative sequencei171 – 22656GKKKS…EQPAT → ATASAWRPDALHQRPRTSPG SIGRSKLQLQPSSRDHSSKS RHSGCSLTAPEVTWNQ in isoform 4.
VSP_046421Add
BLAST
Alternative sequencei227 – 17181492Missing in isoform 4.
VSP_046422Add
BLAST
Alternative sequencei1679 – 16824SYSL → RNFL in isoform 2 and isoform 5.
VSP_006927
Alternative sequencei1683 – 171836Missing in isoform 2 and isoform 5.
VSP_006928Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641S → T in AAA87023. 1 Publication
Sequence conflicti196 – 1961D → S in AAA87023. 1 Publication
Sequence conflicti200 – 2001A → G in AAA87023. 1 Publication
Sequence conflicti276 – 29318EDEEE…LEDEG → VGGGGGVVVVVSWKARGE in AAA87023. 1 Publication
Add
BLAST
Sequence conflicti307 – 31812EPEIR…EKPED → SQKYGVMRSQKI in AAA87023. 1 Publication
Add
BLAST
Sequence conflicti336 – 3372EV → DL in AAA87023. 1 Publication
Sequence conflicti371 – 3711T → I in AAA87023. 1 Publication
Sequence conflicti466 – 4672DT → VS in AAA87023. 1 Publication
Sequence conflicti530 – 5301Q → L in BX647310. 1 Publication
Sequence conflicti534 – 55017TQNVY…EEGEA → PRTCMYQAQSRRGRGSR in AAA87023. 1 Publication
Add
BLAST
Sequence conflicti703 – 7031P → PP1 Publication
Sequence conflicti703 – 7031P → PP1 Publication
Sequence conflicti856 – 8561H → R in BX647310. 1 Publication
Sequence conflicti1456 – 14561I → T in BX647310. 1 Publication
Isoform 4 (identifier: Q13029-4)
Sequence conflicti198 – 1981Q → R in BC014468. 1 Publication

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.
ENST00000376048; ENSP00000365216; ENSG00000116731. [Q13029-4]
ENST00000413440; ENSP00000411103; ENSG00000116731.
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 .
ENST00000376048 ; ENSP00000365216 ; ENSG00000116731 . [Q13029-4 ]
ENST00000413440 ; ENSP00000411103 ; ENSG00000116731 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 152 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

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