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Q13029 (PRDM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PRDM2
Synonyms:KMT8, RIZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1718 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

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

Subunit structure

Binds to the retinoblastoma protein (RB). Interacts with GATA3. Ref.6 Ref.11

Subcellular location

Nucleus Ref.1 Ref.2 Ref.8.

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. Ref.2 Ref.7

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Contains 8 C2H2-type zinc fingers.

Contains 1 SET domain.

Sequence caution

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

Alternative products

This entry describes 5 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.
Note: 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.
Note: Produced by alternative initiation at Met-202 of isoform 1.
Isoform 4 (identifier: Q13029-4)

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.
Isoform 5 (identifier: Q13029-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17181718PR domain zinc finger protein 2
PRO_0000041634

Regions

Domain28 – 141114SET
Zinc finger360 – 38223C2H2-type 1
Zinc finger390 – 41223C2H2-type 2
Zinc finger483 – 50624C2H2-type 3
Zinc finger1134 – 115623C2H2-type 4
Zinc finger1162 – 118524C2H2-type 5
Zinc finger1191 – 121424C2H2-type 6
Zinc finger1333 – 135523C2H2-type 7; atypical
Zinc finger1455 – 147824C2H2-type 8; atypical
Region294 – 31623Retinoblastoma protein binding
Motif970 – 97910SH3-binding Potential
Motif985 – 99814SH3-binding Potential
Motif1028 – 105225SH3-binding Potential
Compositional bias268 – 29629Asp/Glu-rich (acidic)
Compositional bias933 – 1049117Pro-rich
Compositional bias1052 – 107423Poly-Ser
Compositional bias1361 – 144787Arg/Lys-rich (basic)

Natural variations

Alternative sequence1 – 201201Missing in isoform 3 and isoform 5.
VSP_018974
Alternative sequence171 – 22656GKKKS…EQPAT → ATASAWRPDALHQRPRTSPG SIGRSKLQLQPSSRDHSSKS RHSGCSLTAPEVTWNQ in isoform 4.
VSP_046421
Alternative sequence227 – 17181492Missing in isoform 4.
VSP_046422
Alternative sequence1679 – 16824SYSL → RNFL in isoform 2 and isoform 5.
VSP_006927
Alternative sequence1683 – 171836Missing in isoform 2 and isoform 5.
VSP_006928
Natural variant2831D → E.
Corresponds to variant rs2076324 [ dbSNP | Ensembl ].
VAR_052929
Natural variant4501S → N.
Corresponds to variant rs17350795 [ dbSNP | Ensembl ].
VAR_052930

Experimental info

Mutagenesis1061C → Y: Reduced histone methyltransferase activity. Ref.8
Mutagenesis1591A → V: Reduced histone methyltransferase activity. Ref.8
Mutagenesis1881I → V: Loss of histone methyltransferase activity. Ref.8
Sequence conflict1641S → T in AAA87023. Ref.6
Sequence conflict1961D → S in AAA87023. Ref.6
Sequence conflict2001A → G in AAA87023. Ref.6
Sequence conflict276 – 29318EDEEE…LEDEG → VGGGGGVVVVVSWKARGE in AAA87023. Ref.6
Sequence conflict307 – 31812EPEIR…EKPED → SQKYGVMRSQKI in AAA87023. Ref.6
Sequence conflict336 – 3372EV → DL in AAA87023. Ref.6
Sequence conflict3711T → I in AAA87023. Ref.6
Sequence conflict466 – 4672DT → VS in AAA87023. Ref.6
Sequence conflict5301Q → L in BX647310. Ref.3
Sequence conflict534 – 55017TQNVY…EEGEA → PRTCMYQAQSRRGRGSR in AAA87023. Ref.6
Sequence conflict7031P → PP Ref.1
Sequence conflict7031P → PP Ref.7
Sequence conflict8561H → R in BX647310. Ref.3
Sequence conflict14561I → T in BX647310. Ref.3
Isoform 4:
Sequence conflict1981Q → R in BC014468. Ref.5

Secondary structure

.................................... 1718
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RIZ1) [UniParc].

Last modified December 21, 2004. Version 3.
Checksum: 536BD68667AFE433

FASTA1,718188,915
        10         20         30         40         50         60 
MNQNTTEPVA ATETLAEVPE HVLRGLPEEV RLFPSAVDKT RIGVWATKPI LKGKKFGPFV 

        70         80         90        100        110        120 
GDKKKRSQVK NNVYMWEVYY PNLGWMCIDA TDPEKGNWLR YVNWACSGEE QNLFPLEINR 

       130        140        150        160        170        180 
AIYYKTLKPI APGEELLVWY NGEDNPEIAA AIEEERASAR SKRSSPKSRK GKKKSQENKN 

       190        200        210        220        230        240 
KGNKIQDIQL KTSEPDFTSA NMRDSAEGPK EDEEKPSASA LEQPATLQEV ASQEVPPELA 

       250        260        270        280        290        300 
TPAPAWEPQP EPDERLEAAA CEVNDLGEEE EEEEEEDEEE EEDDDDDELE DEGEEEASMP 

       310        320        330        340        350        360 
NENSVKEPEI RCDEKPEDLL EEPKTTSEET LEDCSEVTPA MQIPRTKEEA NGDVFETFMF 

       370        380        390        400        410        420 
PCQHCERKFT TKQGLERHMH IHISTVNHAF KCKYCGKAFG TQINRRRHER RHEAGLKRKP 

       430        440        450        460        470        480 
SQTLQPSEDL ADGKASGENV ASKDDSSPPS LGPDCLIMNS EKASQDTINS SVVEENGEVK 

       490        500        510        520        530        540 
ELHPCKYCKK VFGTHTNMRR HQRRVHERHL IPKGVRRKGG LEEPQPPAEQ AQATQNVYVP 

       550        560        570        580        590        600 
STEPEEEGEA DDVYIMDISS NISENLNYYI DGKIQTNNNT SNCDVIEMES ASADLYGINC 

       610        620        630        640        650        660 
LLTPVTVEIT QNIKTTQVPV TEDLPKEPLG STNSEAKKRR TASPPALPKI KAETDSDPMV 

       670        680        690        700        710        720 
PSCSLSLPLS ISTTEAVSFH KEKSVYLSSK LKQLLQTQDK LTPAGISATE IAKLGPVCVS 

       730        740        750        760        770        780 
APASMLPVTS SRFKRRTSSP PSSPQHSPAL RDFGKPSDGK AAWTDAGLTS KKSKLESHSD 

       790        800        810        820        830        840 
SPAWSLSGRD ERETVSPPCF DEYKMSKEWT ASSAFSSVCN QQPLDLSSGV KQKAEGTGKT 

       850        860        870        880        890        900 
PVQWESVLDL SVHKKHCSDS EGKEFKESHS VQPTCSAVKK RKPTTCMLQK VLLNEYNGID 

       910        920        930        940        950        960 
LPVENPADGT RSPSPCKSLE AQPDPDLGPG SGFPAPTVES TPDVCPSSPA LQTPSLSSGQ 

       970        980        990       1000       1010       1020 
LPPLLIPTDP SSPPPCPPVL TVATPPPPLL PTVPLPAPSS SASPHPCPSP LSNATAQSPL 

      1030       1040       1050       1060       1070       1080 
PILSPTVSPS PSPIPPVEPL MSAASPGPPT LSSSSSSSSS SSSFSSSSSS SSPSPPPLSA 

      1090       1100       1110       1120       1130       1140 
ISSVVSSGDN LEASLPMISF KQEELENEGL KPREEPQSAA EQDVVVQETF NKNFVCNVCE 

      1150       1160       1170       1180       1190       1200 
SPFLSIKDLT KHLSIHAEEW PFKCEFCVQL FKDKTDLSEH RFLLHGVGNI FVCSVCKKEF 

      1210       1220       1230       1240       1250       1260 
AFLCNLQQHQ RDLHPDKVCT HHEFESGTLR PQNFTDPSKA HVEHMQSLPE DPLETSKEEE 

      1270       1280       1290       1300       1310       1320 
ELNDSSEELY TTIKIMASGI KTKDPDVRLG LNQHYPSFKP PPFQYHHRNP MGIGVTATNF 

      1330       1340       1350       1360       1370       1380 
TTHNIPQTFT TAIRCTKCGK GVDNMPELHK HILACASASD KKRYTPKKNP VPLKQTVQPK 

      1390       1400       1410       1420       1430       1440 
NGVVVLDNSG KNAFRRMGQP KRLNFSVELS KMSSNKLKLN ALKKKNQLVQ KAILQKNKSA 

      1450       1460       1470       1480       1490       1500 
KQKADLKNAC ESSSHICPYC NREFTYIGSL NKHAAFSCPK KPLSPPKKKV SHSSKKGGHS 

      1510       1520       1530       1540       1550       1560 
SPASSDKNSN SNHRRRTADA EIKMQSMQTP LGKTRARSSG PTQVPLPSSS FRSKQNVKFA 

      1570       1580       1590       1600       1610       1620 
ASVKSKKPSS SSLRNSSPIR MAKITHVEGK KPKAVAKNHS AQLSSKTSRS LHVRVQKSKA 

      1630       1640       1650       1660       1670       1680 
VLQSKSTLAS KKRTDRFNIK SRERSGGPVT RSLQLAAAAD LSENKREDGS AKQELKDFSY 

      1690       1700       1710 
SLRLASRCSP PAAPYITRQY RKVKAPAAAQ FQGPFFKE 

« Hide

Isoform 2 (MTB-Zf) [UniParc].

Checksum: F353A6402F93712D
Show »

FASTA1,682184,961
Isoform 3 (RIZ2) [UniParc].

Checksum: 2AB9A94179532CE7
Show »

FASTA1,517166,061
Isoform 4 [UniParc].

Checksum: D7CE11A6D48E16D7
Show »

FASTA22625,519
Isoform 5 [UniParc].

Checksum: 87F7398540D3A5F3
Show »

FASTA1,481162,107

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] [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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Structural studies of the SET domain from RIZ1 tumor suppressor."
Briknarova K., Zhou X., Satterthwait A., Hoyt D.W., Ely K.R., Huang S.
Biochem. Biophys. Res. Commun. 366:807-813(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-161, INTERACTION WITH HISTONE H3.
[12]"Structural biology of human H3K9 methyltransferases."
Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., Plotnikov A.N., Schapira M.
PLoS ONE 5:E8570-E8570(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 2-148.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI38902.
RefSeqNP_001007258.1. NM_001007257.2.
NP_001129082.1. NM_001135610.1.
NP_036363.2. NM_012231.4.
NP_056950.2. NM_015866.4.
XP_005246050.1. XM_005245993.1.
XP_005246054.1. XM_005245997.1.
UniGeneHs.371823.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JV0NMR-A1-161[»]
2QPWX-ray1.79A2-148[»]
ProteinModelPortalQ13029.
SMRQ13029. Positions 2-148, 357-504, 1132-1354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113575. 8 interactions.
DIPDIP-428N.
IntActQ13029. 2 interactions.
STRING9606.ENSP00000235372.

PTM databases

PhosphoSiteQ13029.

Polymorphism databases

DMDM56757653.

Proteomic databases

PaxDbQ13029.
PRIDEQ13029.

Protocols and materials databases

DNASU7799.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235372; ENSP00000235372; ENSG00000116731. [Q13029-1]
ENST00000311066; ENSP00000312352; ENSG00000116731. [Q13029-2]
ENST00000343137; ENSP00000341621; ENSG00000116731.
ENST00000376048; ENSP00000365216; ENSG00000116731. [Q13029-4]
ENST00000413440; ENSP00000411103; ENSG00000116731.
GeneID7799.
KEGGhsa:7799.
UCSCuc001avh.3. human. [Q13029-2]
uc001avi.3. human. [Q13029-1]

Organism-specific databases

CTD7799.
GeneCardsGC01P014026.
HGNCHGNC:9347. PRDM2.
HPAHPA005809.
MIM601196. gene.
neXtProtNX_Q13029.
PharmGKBPA33715.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258873.
HOGENOMHOG000231078.
HOVERGENHBG053671.
InParanoidQ13029.
KOK11432.
OMATHTNMRR.
OrthoDBEOG7NW68B.
PhylomeDBQ13029.
TreeFamTF332173.

Gene expression databases

ArrayExpressQ13029.
BgeeQ13029.
CleanExHS_PRDM2.
GenevestigatorQ13029.

Family and domain databases

Gene3D3.30.160.60. 1 hit.
InterProIPR009170. RIZ_retinblastoma-bd_prot.
IPR001214. SET_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00856. SET. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
PIRSFPIRSF002395. RIZ_SET. 1 hit.
SMARTSM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
PROSITEPS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 6 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13029.
GeneWikiPRDM2.
GenomeRNAi7799.
NextBio30170.
PROQ13029.
SOURCESearch...

Entry information

Entry namePRDM2_HUMAN
AccessionPrimary (citable) accession number: Q13029
Secondary accession number(s): B1AJZ4 expand/collapse secondary AC list , B5MC68, Q13149, Q14550, Q5THJ1, Q5VUL9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM