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Q13029

- PRDM2_HUMAN

UniProt

Q13029 - PRDM2_HUMAN

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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

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
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 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

BgeeiQ13029.
CleanExiHS_PRDM2.
ExpressionAtlasiQ13029. baseline and differential.
GenevestigatoriQ13029.

Organism-specific databases

HPAiHPA005809.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi113575. 11 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 – 73Combined sources
Helixi15 – 173Combined sources
Helixi20 – 245Combined sources
Beta strandi27 – 293Combined sources
Beta strandi30 – 345Combined sources
Turni36 – 394Combined sources
Beta strandi41 – 488Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 643Combined sources
Helixi66 – 683Combined sources
Beta strandi72 – 809Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 896Combined sources
Helixi93 – 953Combined sources
Helixi98 – 1014Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi121 – 1288Combined sources
Helixi146 – 15813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JV0NMR-A1-161[»]
2QPWX-ray1.79A2-148[»]
ProteinModelPortaliQ13029.
SMRiQ13029. Positions 2-148, 357-412, 1131-1210, 1266-1298, 1328-1353, 1444-1486.
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.
GeneTreeiENSGT00730000111050.
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

        10         20         30         40         50
MNQNTTEPVA ATETLAEVPE HVLRGLPEEV RLFPSAVDKT RIGVWATKPI
60 70 80 90 100
LKGKKFGPFV GDKKKRSQVK NNVYMWEVYY PNLGWMCIDA TDPEKGNWLR
110 120 130 140 150
YVNWACSGEE QNLFPLEINR AIYYKTLKPI APGEELLVWY NGEDNPEIAA
160 170 180 190 200
AIEEERASAR SKRSSPKSRK GKKKSQENKN KGNKIQDIQL KTSEPDFTSA
210 220 230 240 250
NMRDSAEGPK EDEEKPSASA LEQPATLQEV ASQEVPPELA TPAPAWEPQP
260 270 280 290 300
EPDERLEAAA CEVNDLGEEE EEEEEEDEEE EEDDDDDELE DEGEEEASMP
310 320 330 340 350
NENSVKEPEI RCDEKPEDLL EEPKTTSEET LEDCSEVTPA MQIPRTKEEA
360 370 380 390 400
NGDVFETFMF PCQHCERKFT TKQGLERHMH IHISTVNHAF KCKYCGKAFG
410 420 430 440 450
TQINRRRHER RHEAGLKRKP SQTLQPSEDL ADGKASGENV ASKDDSSPPS
460 470 480 490 500
LGPDCLIMNS EKASQDTINS SVVEENGEVK ELHPCKYCKK VFGTHTNMRR
510 520 530 540 550
HQRRVHERHL IPKGVRRKGG LEEPQPPAEQ AQATQNVYVP STEPEEEGEA
560 570 580 590 600
DDVYIMDISS NISENLNYYI DGKIQTNNNT SNCDVIEMES ASADLYGINC
610 620 630 640 650
LLTPVTVEIT QNIKTTQVPV TEDLPKEPLG STNSEAKKRR TASPPALPKI
660 670 680 690 700
KAETDSDPMV PSCSLSLPLS ISTTEAVSFH KEKSVYLSSK LKQLLQTQDK
710 720 730 740 750
LTPAGISATE IAKLGPVCVS APASMLPVTS SRFKRRTSSP PSSPQHSPAL
760 770 780 790 800
RDFGKPSDGK AAWTDAGLTS KKSKLESHSD SPAWSLSGRD ERETVSPPCF
810 820 830 840 850
DEYKMSKEWT ASSAFSSVCN QQPLDLSSGV KQKAEGTGKT PVQWESVLDL
860 870 880 890 900
SVHKKHCSDS EGKEFKESHS VQPTCSAVKK RKPTTCMLQK VLLNEYNGID
910 920 930 940 950
LPVENPADGT RSPSPCKSLE AQPDPDLGPG SGFPAPTVES TPDVCPSSPA
960 970 980 990 1000
LQTPSLSSGQ LPPLLIPTDP SSPPPCPPVL TVATPPPPLL PTVPLPAPSS
1010 1020 1030 1040 1050
SASPHPCPSP LSNATAQSPL PILSPTVSPS PSPIPPVEPL MSAASPGPPT
1060 1070 1080 1090 1100
LSSSSSSSSS SSSFSSSSSS SSPSPPPLSA ISSVVSSGDN LEASLPMISF
1110 1120 1130 1140 1150
KQEELENEGL KPREEPQSAA EQDVVVQETF NKNFVCNVCE SPFLSIKDLT
1160 1170 1180 1190 1200
KHLSIHAEEW PFKCEFCVQL FKDKTDLSEH RFLLHGVGNI FVCSVCKKEF
1210 1220 1230 1240 1250
AFLCNLQQHQ RDLHPDKVCT HHEFESGTLR PQNFTDPSKA HVEHMQSLPE
1260 1270 1280 1290 1300
DPLETSKEEE ELNDSSEELY TTIKIMASGI KTKDPDVRLG LNQHYPSFKP
1310 1320 1330 1340 1350
PPFQYHHRNP MGIGVTATNF TTHNIPQTFT TAIRCTKCGK GVDNMPELHK
1360 1370 1380 1390 1400
HILACASASD KKRYTPKKNP VPLKQTVQPK NGVVVLDNSG KNAFRRMGQP
1410 1420 1430 1440 1450
KRLNFSVELS KMSSNKLKLN ALKKKNQLVQ KAILQKNKSA KQKADLKNAC
1460 1470 1480 1490 1500
ESSSHICPYC NREFTYIGSL NKHAAFSCPK KPLSPPKKKV SHSSKKGGHS
1510 1520 1530 1540 1550
SPASSDKNSN SNHRRRTADA EIKMQSMQTP LGKTRARSSG PTQVPLPSSS
1560 1570 1580 1590 1600
FRSKQNVKFA ASVKSKKPSS SSLRNSSPIR MAKITHVEGK KPKAVAKNHS
1610 1620 1630 1640 1650
AQLSSKTSRS LHVRVQKSKA VLQSKSTLAS KKRTDRFNIK SRERSGGPVT
1660 1670 1680 1690 1700
RSLQLAAAAD LSENKREDGS AKQELKDFSY SLRLASRCSP PAAPYITRQY
1710
RKVKAPAAAQ FQGPFFKE
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.Curated

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:
EMBLi
GenBanki
DDBJi
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]
uc001avk.3. human.

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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 357-412, 1131-1210, 1266-1298, 1328-1353, 1444-1486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113575. 11 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 ]
uc001avk.3. human.

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.
GeneTreei ENSGT00730000111050.
HOGENOMi HOG000231078.
HOVERGENi HBG053671.
InParanoidi Q13029.
KOi K11432.
OMAi THTNMRR.
OrthoDBi EOG7NW68B.
PhylomeDBi Q13029.
TreeFami TF332173.

Miscellaneous databases

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

Gene expression databases

Bgeei Q13029.
CleanExi HS_PRDM2.
ExpressionAtlasi Q13029. baseline and differential.
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: November 26, 2014
This is version 155 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