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Q96KQ7

- EHMT2_HUMAN

UniProt

Q96KQ7 - EHMT2_HUMAN

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Protein

Histone-lysine N-methyltransferase EHMT2

Gene
EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.6 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi974 – 9741Zinc 1
Metal bindingi974 – 9741Zinc 2
Metal bindingi976 – 9761Zinc 1
Metal bindingi980 – 9801Zinc 1
Metal bindingi980 – 9801Zinc 3
Metal bindingi985 – 9851Zinc 1
Metal bindingi987 – 9871Zinc 2
Metal bindingi1017 – 10171Zinc 2
Metal bindingi1017 – 10171Zinc 3
Metal bindingi1021 – 10211Zinc 2
Metal bindingi1023 – 10231Zinc 3
Metal bindingi1027 – 10271Zinc 3
Binding sitei1067 – 10671Histone H3K9me By similarity
Binding sitei1085 – 10851S-adenosyl-L-methionine
Metal bindingi1115 – 11151Zinc 4
Metal bindingi1168 – 11681Zinc 4
Binding sitei1169 – 11691S-adenosyl-L-methionine; via amide nitrogen
Metal bindingi1170 – 11701Zinc 4
Metal bindingi1175 – 11751Zinc 4

GO - Molecular functioni

  1. C2H2 zinc finger domain binding Source: UniProt
  2. histone-lysine N-methyltransferase activity Source: UniProtKB
  3. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  4. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  5. p53 binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein-lysine N-methyltransferase activity Source: UniProtKB
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA methylation Source: UniProtKB
  2. DNA methylation on cytosine within a CG sequence Source: Ensembl
  3. fertilization Source: Ensembl
  4. histone methylation Source: UniProtKB
  5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  6. organ growth Source: Ensembl
  7. peptidyl-lysine dimethylation Source: UniProtKB
  8. regulation of DNA replication Source: UniProtKB
  9. spermatid development Source: Ensembl
  10. synaptonemal complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase EHMT2 (EC:2.1.1.-, EC:2.1.1.43)
Alternative name(s):
Euchromatic histone-lysine N-methyltransferase 2
HLA-B-associated transcript 8
Histone H3-K9 methyltransferase 3
Short name:
H3-K9-HMTase 3
Lysine N-methyltransferase 1C
Protein G9a
Gene namesi
Name:EHMT2
Synonyms:BAT8, C6orf30, G9A, KMT1C, NG36
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14129. EHMT2.

Subcellular locationi

Nucleus. Chromosome
Note: Associates with euchromatic regions. Does not associate with heterochromatin.1 Publication

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi786 – 7861W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi791 – 7911W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi794 – 7941E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi817 – 8171E → R: Impairs binding to histone H3K9me. 1 Publication
Mutagenesisi824 – 8241W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
Mutagenesisi852 – 8521D → R: Impairs binding to histone H3K9me. 1 Publication

Organism-specific databases

PharmGKBiPA25267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12101209Histone-lysine N-methyltransferase EHMT2PRO_0000186068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei140 – 1401Phosphoserine3 Publications
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei185 – 1851N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
Modified residuei185 – 1851N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
Modified residuei232 – 2321Phosphoserine3 Publications
Modified residuei246 – 2461Phosphoserine4 Publications
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei1204 – 12041Phosphoserine1 Publication
Modified residuei1210 – 12101Phosphothreonine1 Publication

Post-translational modificationi

Methylated at Lys-185; automethylated.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ96KQ7.
PaxDbiQ96KQ7.
PRIDEiQ96KQ7.

Expressioni

Tissue specificityi

Expressed in all tissues examined, with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow.1 Publication

Gene expression databases

ArrayExpressiQ96KQ7.
BgeeiQ96KQ7.
CleanExiHS_EHMT2.
GenevestigatoriQ96KQ7.

Organism-specific databases

HPAiHPA050550.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with EHMT1/GLP. Interacts with GFI1B and WIZ. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with UHRF1. Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GFI1Q996842EBI-744366,EBI-949368
Gfi1Q071203EBI-744366,EBI-4289236From a different organism.
HDAC1Q135473EBI-744366,EBI-301834
KAT2BQ928313EBI-744366,EBI-477430
PRDM5Q9NQX13EBI-744366,EBI-4292031
PRRC2BQ5JSZ52EBI-744366,EBI-744891
REREQ9P2R63EBI-744366,EBI-948076

Protein-protein interaction databases

BioGridi116123. 79 interactions.
DIPiDIP-34461N.
IntActiQ96KQ7. 37 interactions.
MINTiMINT-1441977.
STRINGi9606.ENSP00000397323.

Structurei

Secondary structure

1
1210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi920 – 9245
Turni926 – 9294
Beta strandi931 – 9333
Beta strandi937 – 9437
Beta strandi949 – 9524
Beta strandi957 – 9604
Helixi968 – 9703
Beta strandi977 – 9804
Helixi986 – 9905
Beta strandi1008 – 10103
Beta strandi1021 – 10233
Beta strandi1027 – 10293
Helixi1032 – 10343
Beta strandi1040 – 10445
Beta strandi1046 – 105611
Beta strandi1063 – 10675
Beta strandi1069 – 10735
Helixi1074 – 10774
Beta strandi1086 – 10894
Beta strandi1097 – 11059
Helixi1107 – 11104
Beta strandi1118 – 112710
Beta strandi1135 – 11428
Helixi1156 – 11627
Turni1163 – 11653
Beta strandi1176 – 11783
Helixi1179 – 118810

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8JX-ray1.80A/B/C/D913-1193[»]
3DM1X-ray2.40B/D/F/H179-190[»]
3K5KX-ray1.70A/B913-1193[»]
3RJWX-ray2.56A/B913-1193[»]
4NVQX-ray2.03A/B913-1193[»]
ProteinModelPortaliQ96KQ7.
SMRiQ96KQ7. Positions 632-908, 922-1192.

Miscellaneous databases

EvolutionaryTraceiQ96KQ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati649 – 67830ANK 1Add
BLAST
Repeati684 – 71330ANK 2Add
BLAST
Repeati717 – 74630ANK 3Add
BLAST
Repeati750 – 78031ANK 4Add
BLAST
Repeati784 – 81330ANK 5Add
BLAST
Repeati817 – 84630ANK 6Add
BLAST
Repeati850 – 87930ANK 7Add
BLAST
Domaini972 – 103564Pre-SETAdd
BLAST
Domaini1038 – 1155118SETAdd
BLAST
Domaini1164 – 118017Post-SETAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni817 – 8193Histone H3K9me binding By similarity
Regioni1048 – 10503S-adenosyl-L-methionine binding
Regioni1074 – 109320Interaction with histone H3 By similarityAdd
BLAST
Regioni1112 – 11132S-adenosyl-L-methionine binding
Regioni1154 – 11574Interaction with histone H3 By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1312Poly-AlaAdd
BLAST
Compositional biasi160 – 1634Poly-Ala
Compositional biasi300 – 32627Poly-GluAdd
BLAST

Domaini

The SET domain mediates interaction with WIZ.1 Publication
The ANK repeats bind H3K9me1 and H3K9me2.1 Publication
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.1 Publication

Sequence similaritiesi

Contains 7 ANK repeats.
Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOVERGENiHBG028394.
KOiK11420.
PhylomeDBiQ96KQ7.
TreeFamiTF106443.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00023. Ank. 6 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q96KQ7-1) [UniParc]FASTAAdd to Basket

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

MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET     50
LPKATPDSLE PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG 100
DLRGGRILLG HATKSFPSSP SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR 150
LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV HRARKTMSKP GNGQPPVPEK 200
RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL GSARRSGEVT 250
LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 300
EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS 350
PWVKPSRKRR KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL 400
SPNHAGVSND TSSLETERGF EELPLCSCRM EAPKIDRISE RAGHKCMATE 450
SVDGELSGCN AAILKRETMR PSSRVALMVL CETHRARMVK HHCCPGCGYF 500
CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA SEAQEVTIPR 550
GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA 600
DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH 650
PRQLYLSVKQ GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI 700
CHVLLQAGAN INAVDKQQRT PLMEAVVNNH LEVARYMVQR GGCVYSKEED 750
GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA QDSGGWTPII WAAEHKHIEV 800
IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA RCDLHAVNYH 850
GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA 900
LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY 950
KYISENCETS TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG 1000
RLLQEFNKIE PPLIFECNQA CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW 1050
GVRALQTIPQ GTFICEYVGE LISDAEADVR EDDSYLFDLD NKDGEVYCID 1100
ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS SRDIRTGEEL 1150
GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP 1200
ELGSLPPVNT 1210
Length:1,210
Mass (Da):132,370
Last modified:October 17, 2006 - v3
Checksum:iA6C5DC6B72801520
GO
Isoform 2 (identifier: Q96KQ7-2) [UniParc]FASTAAdd to Basket

Also known as: NG36G9a-SPI

The sequence of this isoform differs from the canonical sequence as follows:
     373-406: Missing.

Show »
Length:1,176
Mass (Da):129,019
Checksum:i887FC5E322B772B9
GO
Isoform 3 (identifier: Q96KQ7-3) [UniParc]FASTAAdd to Basket

Also known as: NG36

The sequence of this isoform differs from the canonical sequence as follows:
     195-202: PPVPEKRP → VSGMGEMG
     203-1210: Missing.

Show »
Length:202
Mass (Da):19,864
Checksum:i339618C3DA895788
GO

Sequence cautioni

The sequence AAH02686.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH09351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH18718.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH20970.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAA49491.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAD21811.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAD21812.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence BAB63294.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence BAB63295.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551T → N.4 Publications
Corresponds to variant rs7887 [ dbSNP | Ensembl ].
VAR_027973
Natural varianti1165 – 11651Y → F.
Corresponds to variant rs13919 [ dbSNP | Ensembl ].
VAR_027974

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 2028PPVPEKRP → VSGMGEMG in isoform 3. VSP_002212
Alternative sequencei203 – 12101008Missing in isoform 3. VSP_002213Add
BLAST
Alternative sequencei373 – 40634Missing in isoform 2. VSP_002211Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781P → S in CAC86666. 1 Publication
Sequence conflicti985 – 9851C → R in CAC86666. 1 Publication
Sequence conflicti994 – 9941C → R in CAA49491. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ315532 mRNA. Translation: CAC86666.1.
AK056936 mRNA. Translation: BAB71314.1.
AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems.
AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems.
BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems.
AL662834 Genomic DNA. Translation: CAI17747.2.
AL662834 Genomic DNA. Translation: CAI17748.1.
AL671762 Genomic DNA. Translation: CAI18224.2.
AL671762 Genomic DNA. Translation: CAI18226.2.
AL844853 Genomic DNA. Translation: CAI41852.1.
AL844853 Genomic DNA. Translation: CAI41853.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07473.1.
CR388219, CR388202 Genomic DNA. Translation: CAQ07474.1.
CR936237 Genomic DNA. Translation: CAQ09159.1.
CR759784 Genomic DNA. Translation: CAQ09311.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09508.1.
CR388202, CR388219 Genomic DNA. Translation: CAQ09509.1.
CH471081 Genomic DNA. Translation: EAX03542.1.
BC002686 mRNA. Translation: AAH02686.2. Different initiation.
BC009351 mRNA. Translation: AAH09351.1. Different initiation.
BC018718 mRNA. Translation: AAH18718.1. Different initiation.
BC020970 mRNA. Translation: AAH20970.2. Different initiation.
X69838 mRNA. Translation: CAA49491.1. Different initiation.
CCDSiCCDS4725.1. [Q96KQ7-1]
CCDS4726.1. [Q96KQ7-2]
RefSeqiNP_001276342.1. NM_001289413.1.
NP_006700.3. NM_006709.4. [Q96KQ7-1]
NP_079532.5. NM_025256.6. [Q96KQ7-2]
UniGeneiHs.709218.

Genome annotation databases

EnsembliENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
ENST00000420336; ENSP00000396119; ENSG00000238134.
ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
ENST00000421926; ENSP00000416957; ENSG00000232045.
ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
GeneIDi10919.
KEGGihsa:10919.
UCSCiuc003nxz.1. human. [Q96KQ7-1]
uc003nya.1. human. [Q96KQ7-2]
uc003nyb.1. human. [Q96KQ7-3]

Polymorphism databases

DMDMi116241348.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ315532 mRNA. Translation: CAC86666.1 .
AK056936 mRNA. Translation: BAB71314.1 .
AF134726 Genomic DNA. Translation: AAD21811.1 . Sequence problems.
AF134726 Genomic DNA. Translation: AAD21812.1 . Sequence problems.
BA000025 Genomic DNA. Translation: BAB63294.1 . Sequence problems.
BA000025 Genomic DNA. Translation: BAB63295.1 . Sequence problems.
AL662834 Genomic DNA. Translation: CAI17747.2 .
AL662834 Genomic DNA. Translation: CAI17748.1 .
AL671762 Genomic DNA. Translation: CAI18224.2 .
AL671762 Genomic DNA. Translation: CAI18226.2 .
AL844853 Genomic DNA. Translation: CAI41852.1 .
AL844853 Genomic DNA. Translation: CAI41853.1 .
CR388219 , CR388202 Genomic DNA. Translation: CAQ07473.1 .
CR388219 , CR388202 Genomic DNA. Translation: CAQ07474.1 .
CR936237 Genomic DNA. Translation: CAQ09159.1 .
CR759784 Genomic DNA. Translation: CAQ09311.1 .
CR388202 , CR388219 Genomic DNA. Translation: CAQ09508.1 .
CR388202 , CR388219 Genomic DNA. Translation: CAQ09509.1 .
CH471081 Genomic DNA. Translation: EAX03542.1 .
BC002686 mRNA. Translation: AAH02686.2 . Different initiation.
BC009351 mRNA. Translation: AAH09351.1 . Different initiation.
BC018718 mRNA. Translation: AAH18718.1 . Different initiation.
BC020970 mRNA. Translation: AAH20970.2 . Different initiation.
X69838 mRNA. Translation: CAA49491.1 . Different initiation.
CCDSi CCDS4725.1. [Q96KQ7-1 ]
CCDS4726.1. [Q96KQ7-2 ]
RefSeqi NP_001276342.1. NM_001289413.1.
NP_006700.3. NM_006709.4. [Q96KQ7-1 ]
NP_079532.5. NM_025256.6. [Q96KQ7-2 ]
UniGenei Hs.709218.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O8J X-ray 1.80 A/B/C/D 913-1193 [» ]
3DM1 X-ray 2.40 B/D/F/H 179-190 [» ]
3K5K X-ray 1.70 A/B 913-1193 [» ]
3RJW X-ray 2.56 A/B 913-1193 [» ]
4NVQ X-ray 2.03 A/B 913-1193 [» ]
ProteinModelPortali Q96KQ7.
SMRi Q96KQ7. Positions 632-908, 922-1192.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116123. 79 interactions.
DIPi DIP-34461N.
IntActi Q96KQ7. 37 interactions.
MINTi MINT-1441977.
STRINGi 9606.ENSP00000397323.

Chemistry

BindingDBi Q96KQ7.
ChEMBLi CHEMBL6032.
GuidetoPHARMACOLOGYi 2652.

Polymorphism databases

DMDMi 116241348.

Proteomic databases

MaxQBi Q96KQ7.
PaxDbi Q96KQ7.
PRIDEi Q96KQ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375530 ; ENSP00000364680 ; ENSG00000204371 . [Q96KQ7-2 ]
ENST00000375537 ; ENSP00000364687 ; ENSG00000204371 . [Q96KQ7-1 ]
ENST00000383372 ; ENSP00000372863 ; ENSG00000206376 . [Q96KQ7-2 ]
ENST00000383373 ; ENSP00000372864 ; ENSG00000206376 . [Q96KQ7-1 ]
ENST00000420336 ; ENSP00000396119 ; ENSG00000238134 .
ENST00000420874 ; ENSP00000411035 ; ENSG00000236759 . [Q96KQ7-2 ]
ENST00000421926 ; ENSP00000416957 ; ENSG00000232045 .
ENST00000429506 ; ENSP00000406110 ; ENSG00000227333 . [Q96KQ7-1 ]
ENST00000450075 ; ENSP00000392305 ; ENSG00000236759 . [Q96KQ7-1 ]
ENST00000450229 ; ENSP00000400838 ; ENSG00000227333 . [Q96KQ7-2 ]
GeneIDi 10919.
KEGGi hsa:10919.
UCSCi uc003nxz.1. human. [Q96KQ7-1 ]
uc003nya.1. human. [Q96KQ7-2 ]
uc003nyb.1. human. [Q96KQ7-3 ]

Organism-specific databases

CTDi 10919.
GeneCardsi GC06M031847.
GC06Mi31858.
GC06Mj31835.
GC06Mk31829.
GC06Mm31924.
GC06Mn31837.
H-InvDB HIX0166078.
HIX0166345.
HIX0167369.
HIX0184162.
HGNCi HGNC:14129. EHMT2.
HPAi HPA050550.
MIMi 604599. gene.
neXtProti NX_Q96KQ7.
PharmGKBi PA25267.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOVERGENi HBG028394.
KOi K11420.
PhylomeDBi Q96KQ7.
TreeFami TF106443.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSi EHMT2. human.
EvolutionaryTracei Q96KQ7.
GeneWikii EHMT2.
GenomeRNAii 10919.
NextBioi 41475.
PROi Q96KQ7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96KQ7.
Bgeei Q96KQ7.
CleanExi HS_EHMT2.
Genevestigatori Q96KQ7.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF00023. Ank. 6 hits.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions."
    Brown S.E., Campbell R.D., Sanderson C.M.
    Mamm. Genome 12:916-924(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANT ASN-55.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Salivary gland.
  3. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
    Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., Oka A., Inoko H.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
  7. "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] OF 6-1210 (ISOFORM 1), VARIANT ASN-55.
    Tissue: Muscle and Uterus.
  8. "The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats."
    Milner C.M., Campbell R.D.
    Biochem. J. 290:811-818(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, FUNCTION.
    Tissue: Histiocytic lymphoma.
  9. "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3."
    Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.
    J. Biol. Chem. 276:25309-25317(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
  10. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
    Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
    Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EHMT1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
  11. "Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin."
    Vassen L., Fiolka K., Moeroey T.
    EMBO J. 25:2409-2419(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GFI1B.
  12. "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
    Ueda J., Tachibana M., Ikura T., Shinkai Y.
    J. Biol. Chem. 281:20120-20128(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WIZ AND EHMT1.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
    Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
    Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDYL AND REST, IDENTIFICATION IN A COMPLEX WITH REST; CDYL; SETB1; EHMT1 AND WIZ.
  16. Cited for: FUNCTION, METHYLATION AT LYS-185, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "The ankyrin repeats of G9a and GLP histone methyltransferases are mono-and dimethyllysine binding modules."
    Collins R.E., Northrop J.P., Horton J.R., Lee D.Y., Zhang X., Stallcup M.R., Cheng X.
    Nat. Struct. Mol. Biol. 15:245-250(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN ANK REPEATS, MUTAGENESIS OF TRP-786; TRP-791; GLU-794; GLU-817; TRP-824 AND ASP-852.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; SER-246 AND THR-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells."
    Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.
    Nucleic Acids Res. 37:493-505(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UHRF1.
  21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. Cited for: FUNCTION, INTERACTION WITH TP53.
  23. Erratum
    Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., Reinberg D., Berger S.L.
    J. Biol. Chem. 285:18122-18122(2010)
  24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
    Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
    Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARCAD1.
  26. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232; SER-246; SER-413 AND SER-1204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA."
    Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.
    Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiEHMT2_HUMAN
AccessioniPrimary (citable) accession number: Q96KQ7
Secondary accession number(s): B0UZY2
, Q14349, Q5JP83, Q5JQ92, Q5JQA1, Q5JQG3, Q6PK06, Q96MH5, Q96QD0, Q9UQL8, Q9Y331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 149 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

Caution

While NG36 and G9a were originally thought to derive from 2 separate genes, all G9A transcripts also contain the in frame coding sequence of NG36 (1 Publication).
It is uncertain whether Met-1 or Met-21 is the initiator methionine.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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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