8HPO,8I03


Conserved Protein Domain Family
ING

?
pfam12998: ING (This model is not part of the current CDD release)
Inhibitor of growth proteins N-terminal histone-binding
Histones undergo numerous post-translational modifications, including acetylation and methylation, at residues which are then probable docking sites for various chromatin remodelling complexes. Inhibitor of growth proteins (INGs) specifically bind to residues that have been thus modified. INGs carry a well-characterised C-terminal PHD-type zinc-finger domain, binding with lysine 4-tri-methylated histone H3 (H3K4me3), as well as this N-terminal domain that binds unmodified H3 tails. Although these two regions can bind histones independently, together they increase the apparent association of the ING for the H3 tail.
Statistics
?
PSSM-Id: 520557
Aligned: 66 rows
Threshold Bit Score: 65.2442
Created: 16-Feb-2025
Updated: 28-Apr-2025
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
8HPO_C        10 GLNDITDVLEEFPLATSRYLTLLHEIDAKCVHSMPNLNERIDKFL----------KKDFNKDHQTQVRLLN------NIN 73  Saccharomyces c...
Q9C117        12 LLIQLADALEAIPGDLSKNFTEVRFLEAELKDVYSQALSSIDDLL------------NRDTSVERRNLVAR------NLS 73  Schizosaccharom...
O74736        11 ALNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVL-----------------KNEKNDELSgeerceRLQ 73  Schizosaccharom...
Q6BM01        27 GLNDISDAFEALPLDLIKYFTLLKEIDAKYINTVPVINRNIKSYIdrlhitknspPGMKEMNKPTKIDKLT------VIR 100 Debaryomyces ha...
XP_002494118  49 GLNDITDSFEAFPLELIRYFTLLKEIDAKTVQSVPLLITYIKRFL------------QMSKTHPKREQLLH------EIR 110
Q6C6K6        23 GLNDLTDALEALPLETVRHFTLLREIDAKCTTTTPLVADLIAKFLaipp--aakdDPECAKKTEERENMLL------EIR 94  Yarrowia lipoly...
CCJ28227      17 SLNDFTDAIEALPMDLTRNFTLLREVDAKVSSLQHLISSSISNLL-----------TNTNSFQETKSISSS------KLQ 79 
CCJ28641      17 SLNDFTDAIEALPMDLTRNFTLLREVDAKVSSLQHLISSSISNLL-----------TNTNSFQETKSISSS------KLQ 79 
XP_007875053  17 SLNDFIDAIEALPIDLTRIFTLLREVDAKVSNLEHLISSSISNLL-----------ANTESFQENKSICIS------RLR 79 
8I03_H        11 aLNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVL----------K-NEKNDELSGEERCE------RLQ 73  fission yeast
8HPO_C        74 KIYEELMPSLEEKMHVSSIMLDNLDRLTSRLELAYEVA 111 Saccharomyces cerevisiae S288C
Q9C117        74 LLLKSDDVQTRKKSHIAMYAEAITHSNVLRLEHCYQKM 111 Schizosaccharomyces pombe 972h-
O74736        74 KTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYV 111 Schizosaccharomyces pombe 972h-
Q6BM01       101 DKIHEIIPCLEEKMHVTSVATDLLHKHLYRINADYKLI 138 Debaryomyces hansenii
XP_002494118 111 ELIKELMPCLEEKMHVATIAADAVARHVKRIDSDFELI 148
Q6C6K6        95 GLIRELMPCLEEKMHVAGVAAEAVARHISRIDADYELI 132 Yarrowia lipolytica
CCJ28227      80 SLLIQIIPYADEKISLASSTRDAVKKHLKRLDLDFSLI 117
CCJ28641      80 SLLIQIIPYADEKISLASSTRDAVKKHLKRLDLDFSLI 117
XP_007875053  80 SLLIQIIPYADEKISVASSARDIIKKHLKRLDSDFSLI 117
8I03_H        74 KTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYV 111 fission yeast
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap