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Protein

Lysine-specific demethylase PHF2

Gene

PHF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA.3 Publications

Enzyme regulationi

Enzymatically inactive by itself, and become active following phosphorylation by PKA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei193Alpha-ketoglutarate1
Binding sitei246Alpha-ketoglutarate1
Metal bindingi249Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi251Iron; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei259Alpha-ketoglutarate1
Binding sitei266Alpha-ketoglutarate1
Metal bindingi321Iron; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei321Alpha-ketoglutarate1
Binding sitei323Alpha-ketoglutarate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri5 – 56PHD-typePROSITE-ProRule annotationAdd BLAST52

GO - Molecular functioni

  • dioxygenase activity Source: UniProtKB-KW
  • histone demethylase activity Source: Reactome
  • histone demethylase activity (H3-K9 specific) Source: UniProtKB
  • iron ion binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • liver development Source: UniProtKB
  • negative regulation of chromatin silencing at rDNA Source: UniProtKB
  • protein demethylation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-32922-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase PHF2 (EC:1.14.11.-)
Alternative name(s):
GRC5
PHD finger protein 2
Gene namesi
Name:PHF2Imported
Synonyms:CENP-351 Publication, KIAA0662
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:8920. PHF2.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • kinetochore Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7Y → A: Abolishes binding to H3K4me2 and H3K4me3. 1 Publication1
Mutagenesisi29W → A: Abolishes binding to H3K4me2 and H3K4me3. 1 Publication1
Mutagenesisi249H → A: Abolishes demethylase activity. 1 Publication1
Mutagenesisi321Y → H: Does not alter iron-binding nor activates histone demethylase activity. 1 Publication1
Mutagenesisi757S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056. 1 Publication1
Mutagenesisi899S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056. 1 Publication1
Mutagenesisi954S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056. 1 Publication1
Mutagenesisi1056S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954. 1 Publication1

Organism-specific databases

DisGeNETi5253.
OpenTargetsiENSG00000197724.
PharmGKBiPA33260.

Polymorphism and mutation databases

BioMutaiPHF2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000592901 – 1096Lysine-specific demethylase PHF2Add BLAST1096

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei474PhosphoserineCombined sources1
Modified residuei479PhosphothreonineCombined sources1
Modified residuei539PhosphoserineCombined sources1
Modified residuei655PhosphoserineCombined sources1
Modified residuei681PhosphoserineCombined sources1
Modified residuei705PhosphoserineCombined sources1
Modified residuei720N6-acetyllysineBy similarity1
Modified residuei728PhosphotyrosineBy similarity1
Modified residuei730PhosphoserineBy similarity1
Modified residuei733PhosphoserineBy similarity1
Modified residuei734PhosphoserineBy similarity1
Modified residuei738PhosphoserineBy similarity1
Modified residuei879PhosphoserineBy similarity1
Modified residuei882PhosphoserineCombined sources1
Modified residuei899PhosphoserineCombined sources1
Modified residuei1056Phosphoserine; by PKA1 Publication1

Post-translational modificationi

Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75151.
MaxQBiO75151.
PaxDbiO75151.
PeptideAtlasiO75151.
PRIDEiO75151.

PTM databases

iPTMnetiO75151.
PhosphoSitePlusiO75151.

Expressioni

Tissue specificityi

Widely expressed, including in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000197724.
CleanExiHS_PHF2.
ExpressionAtlasiO75151. baseline and differential.
GenevisibleiO75151. HS.

Organism-specific databases

HPAiHPA010831.

Interactioni

Subunit structurei

Component of the PHF2-ARID5B complex, at least composed of PHF2 and ARID5B. Interacts with HNF4A and NR1H4.3 Publications

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111272. 5 interactors.
IntActiO75151. 1 interactor.
STRINGi9606.ENSP00000352185.

Structurei

Secondary structure

11096
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 11Combined sources4
Beta strandi20 – 22Combined sources3
Turni24 – 26Combined sources3
Beta strandi29 – 31Combined sources3
Helixi32 – 35Combined sources4
Turni39 – 41Combined sources3
Helixi42 – 44Combined sources3
Beta strandi45 – 47Combined sources3
Helixi51 – 57Combined sources7
Helixi87 – 95Combined sources9
Helixi101 – 103Combined sources3
Beta strandi105 – 107Combined sources3
Helixi110 – 112Combined sources3
Helixi115 – 121Combined sources7
Beta strandi127 – 131Combined sources5
Turni133 – 136Combined sources4
Helixi146 – 153Combined sources8
Beta strandi158 – 163Combined sources6
Turni164 – 166Combined sources3
Beta strandi169 – 173Combined sources5
Helixi174 – 181Combined sources8
Beta strandi190 – 196Combined sources7
Helixi201 – 205Combined sources5
Helixi210 – 215Combined sources6
Helixi217 – 221Combined sources5
Beta strandi236 – 240Combined sources5
Beta strandi245 – 249Combined sources5
Helixi252 – 254Combined sources3
Beta strandi256 – 271Combined sources16
Helixi275 – 286Combined sources12
Helixi290 – 292Combined sources3
Helixi295 – 298Combined sources4
Beta strandi303 – 308Combined sources6
Beta strandi312 – 315Combined sources4
Beta strandi320 – 336Combined sources17
Helixi339 – 341Combined sources3
Helixi342 – 355Combined sources14
Beta strandi359 – 361Combined sources3
Helixi366 – 387Combined sources22
Helixi393 – 409Combined sources17
Turni412 – 414Combined sources3
Helixi415 – 418Combined sources4
Helixi419 – 421Combined sources3
Helixi428 – 443Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KQIX-ray1.78A1-70[»]
3PTRX-ray1.95B60-451[»]
3PU3X-ray1.95A/B60-451[»]
3PU8X-ray1.94A/B60-451[»]
3PUAX-ray1.89A60-451[»]
3PUSX-ray2.08A/B60-451[»]
ProteinModelPortaliO75151.
SMRiO75151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini197 – 353JmjCPROSITE-ProRule annotationAdd BLAST157

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi472 – 518Pro-richAdd BLAST47
Compositional biasi487 – 648Lys-richAdd BLAST162
Compositional biasi960 – 1020Ser/Thr-richAdd BLAST61

Domaini

The PHD-type zinc finger mediates the binding to H3K4me2 and H3K4me3.1 Publication

Sequence similaritiesi

Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri5 – 56PHD-typePROSITE-ProRule annotationAdd BLAST52

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
ENOG410Y2FD. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000231232.
HOVERGENiHBG045631.
InParanoidiO75151.
KOiK19414.
OMAiEAHTKEA.
OrthoDBiEOG091G09DB.
PhylomeDBiO75151.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC
60 70 80 90 100
PNCEKTHGKS TLKKKRTWHK HGPGQAPDVK PVQNGSQLFI KELRSRTFPS
110 120 130 140 150
AEDVVARVPG SQLTLGYMEE HGFTEPILVP KKDGLGLAVP APTFYVSDVE
160 170 180 190 200
NYVGPERSVD VTDVTKQKDC KMKLKEFVDY YYSTNRKRVL NVTNLEFSDT
210 220 230 240 250
RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC VKDSYTDFHI
260 270 280 290 300
DSGGASAWYH VLKGEKTFYL IRPASANISL YERWRSASNH SEMFFADQVD
310 320 330 340 350
KCYKCIVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE
360 370 380 390 400
VERRLKLGSL TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK
410 420 430 440 450
ILNGAFRSWT KKQALAEHED ELPEHFKPSQ LIKDLAKEIR LSENASKAVR
460 470 480 490 500
PEVNTVASSD EVCDGDREKE EPPSPIEATP PQSLLEKVSK KKTPKTVKMP
510 520 530 540 550
KPSKIPKPPK PPKPPRPPKT LKLKDGGKKK GKKSRESASP TIPNLDLLEA
560 570 580 590 600
HTKEALTKME PPKKGKATKS VLSVPNKDVV HMQNDVERLE IREQTKSKSE
610 620 630 640 650
AKWKYKNSKP DSLLKMEEEQ KLEKSPLAGN KDNKFSFSFS NKKLLGSKAL
660 670 680 690 700
RPPTSPGVFG ALQNFKEDKP KPVRDEYEYV SDDGELKIDE FPIRRKKNAP
710 720 730 740 750
KRDLSFLLDK KAVLPTPVTK PKLDSAAYKS DDSSDEGSLH IDTDTKPGRN
760 770 780 790 800
ARVKKESGSS AAGILDLLQA SEEVGALEYN PSSQPPASPS TQEAIQGMLS
810 820 830 840 850
MANLQASDSC LQTTWGAGQA KGSSLAAHGA RKNGGGSGKS AGKRLLKRAA
860 870 880 890 900
KNSVDLDDYE EEQDHLDACF KDSDYVYPSL ESDEDNPIFK SRSKKRKGSD
910 920 930 940 950
DAPYSPTARV GPSVPRQDRP VREGTRVASI ETGLAAAAAK LSQQEEQKSK
960 970 980 990 1000
KKKSAKRKLT PNTTSPSTST SISAGTTSTS TTPASTTPAS TTPASTSTAS
1010 1020 1030 1040 1050
SQASQEGSSP EPPPESHSSS LADHEYTAAG TFTGAQAGRT SQPMAPGVFL
1060 1070 1080 1090
TQRRPSASSP NNNTAAKGKR TKKGMATAKQ RLGKILKIHR NGKLLL
Length:1,096
Mass (Da):120,775
Last modified:November 25, 2008 - v4
Checksum:iDD088363DB76674D
GO

Sequence cautioni

The sequence BAA31637 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19 – 41FMIEC…VEEEE → PRAARPPARPGPTRAAQRRG RAT in BAA31637 (PubMed:9734811).CuratedAdd BLAST23
Sequence conflicti75 – 76QA → PT in AAD21791 (PubMed:10051327).Curated2
Sequence conflicti100S → R in BAA31637 (PubMed:9734811).Curated1
Sequence conflicti106A → S in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti115L → V in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti621K → R in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti633Missing in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti642K → R in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti654T → S in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti664N → S in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti670P → A in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti698N → S in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti712 – 719AVLPTPVT → EALLMPTS in AAD21791 (PubMed:10051327).Curated8
Sequence conflicti727A → V in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti752R → K in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti782S → N in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti817A → T in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti823S → G in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti833N → I in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti837 – 841SGKSA → NKGT in AAD21791 (PubMed:10051327).Curated5
Sequence conflicti849A → T in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti857D → E in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti862Missing in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti888I → V in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti949 – 950SK → NR in AAD21791 (PubMed:10051327).Curated2
Sequence conflicti954 – 955SA → NT in AAD21791 (PubMed:10051327).Curated2
Sequence conflicti959 – 960LT → PA in AAD21791 (PubMed:10051327).Curated2
Sequence conflicti964T → A in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti968T → I in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti972I → ASASTGTT in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti975G → S in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti978 – 979ST → PA in AAD21791 (PubMed:10051327).Curated2
Sequence conflicti996T → TTPAST in BAA31637 (PubMed:9734811).Curated1
Sequence conflicti996T → TTPAST in CAD38938 (PubMed:17974005).Curated1
Sequence conflicti1033 – 1035TGA → SGS in AAD21791 (PubMed:10051327).Curated3
Sequence conflicti1040T → A in AAD21791 (PubMed:10051327).Curated1
Sequence conflicti1063Missing in AAD21791 (PubMed:10051327).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04755356T → P.Corresponds to variant rs34279404dbSNPEnsembl.1
Natural variantiVAR_0515981058S → L.Corresponds to variant rs35236745dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043725 mRNA. Translation: AAD21791.1.
AB014562 mRNA. Translation: BAA31637.2. Different initiation.
AL353629, AL359181 Genomic DNA. Translation: CAI96110.1.
AL359181, AL353629 Genomic DNA. Translation: CAI96111.1.
CH471089 Genomic DNA. Translation: EAW62867.1.
AL834263 mRNA. Translation: CAD38938.1.
CCDSiCCDS35069.1.
PIRiT00369.
RefSeqiNP_005383.3. NM_005392.3.
UniGeneiHs.211441.

Genome annotation databases

EnsembliENST00000359246; ENSP00000352185; ENSG00000197724.
GeneIDi5253.
KEGGihsa:5253.
UCSCiuc004aub.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043725 mRNA. Translation: AAD21791.1.
AB014562 mRNA. Translation: BAA31637.2. Different initiation.
AL353629, AL359181 Genomic DNA. Translation: CAI96110.1.
AL359181, AL353629 Genomic DNA. Translation: CAI96111.1.
CH471089 Genomic DNA. Translation: EAW62867.1.
AL834263 mRNA. Translation: CAD38938.1.
CCDSiCCDS35069.1.
PIRiT00369.
RefSeqiNP_005383.3. NM_005392.3.
UniGeneiHs.211441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KQIX-ray1.78A1-70[»]
3PTRX-ray1.95B60-451[»]
3PU3X-ray1.95A/B60-451[»]
3PU8X-ray1.94A/B60-451[»]
3PUAX-ray1.89A60-451[»]
3PUSX-ray2.08A/B60-451[»]
ProteinModelPortaliO75151.
SMRiO75151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111272. 5 interactors.
IntActiO75151. 1 interactor.
STRINGi9606.ENSP00000352185.

PTM databases

iPTMnetiO75151.
PhosphoSitePlusiO75151.

Polymorphism and mutation databases

BioMutaiPHF2.

Proteomic databases

EPDiO75151.
MaxQBiO75151.
PaxDbiO75151.
PeptideAtlasiO75151.
PRIDEiO75151.

Protocols and materials databases

DNASUi5253.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359246; ENSP00000352185; ENSG00000197724.
GeneIDi5253.
KEGGihsa:5253.
UCSCiuc004aub.4. human.

Organism-specific databases

CTDi5253.
DisGeNETi5253.
GeneCardsiPHF2.
H-InvDBHIX0008184.
HGNCiHGNC:8920. PHF2.
HPAiHPA010831.
MIMi604351. gene.
neXtProtiNX_O75151.
OpenTargetsiENSG00000197724.
PharmGKBiPA33260.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1633. Eukaryota.
ENOG410Y2FD. LUCA.
GeneTreeiENSGT00550000074396.
HOGENOMiHOG000231232.
HOVERGENiHBG045631.
InParanoidiO75151.
KOiK19414.
OMAiEAHTKEA.
OrthoDBiEOG091G09DB.
PhylomeDBiO75151.
TreeFamiTF106480.

Enzyme and pathway databases

BioCyciZFISH:G66-32922-MONOMER.
ReactomeiR-HSA-3214842. HDMs demethylate histones.

Miscellaneous databases

ChiTaRSiPHF2. human.
EvolutionaryTraceiO75151.
GenomeRNAii5253.
PROiO75151.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197724.
CleanExiHS_PHF2.
ExpressionAtlasiO75151. baseline and differential.
GenevisibleiO75151. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHF2_HUMAN
AccessioniPrimary (citable) accession number: O75151
Secondary accession number(s): Q4VXG0, Q8N3K2, Q9Y6N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 133 of the entry and version 4 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

Caution

In contrast to the related histone demethylases JHDM1D and PHF8, the conserved active His in position 321 is replaced by a Tyr. However, the presence of a Tyr residue neither affects binding to the catalytic iron nor abolishes demethylase activity (PubMed:21167174).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.