CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023247
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inhibitor of growth protein 4 
Protein Synonyms/Alias
 p29ING4 
Gene Name
 ING4 
Gene Synonyms/Alias
 My036 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
127DYDSSSSKEGRTQKEacetylation[1]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1). 
Sequence Annotation
 ZN_FING 196 245 PHD-type.
 MOTIF 127 148 Bipartite nuclear localization signal.
 BINDING 198 198 Histone H3K4me3 (By similarity).
 BINDING 209 209 Histone H3K4me3 (By similarity).
 BINDING 213 213 Histone H3K4me3 (By similarity).
 BINDING 221 221 Histone H3K4me3 (By similarity).
 MOD_RES 112 112 N6-acetyllysine.
 MOD_RES 127 127 N6-acetyllysine.
 MOD_RES 129 129 N6-acetyllysine.
 MOD_RES 133 133 Citrulline.
 MOD_RES 146 146 N6-acetyllysine.
 MOD_RES 148 148 N6-acetyllysine.
 MOD_RES 150 150 Phosphoserine (By similarity).
 MOD_RES 156 156 N6-acetyllysine.
 MOD_RES 166 166 Citrulline.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Chromatin regulator; Citrullination; Coiled coil; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 249 AA 
Protein Sequence
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE 60
KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD 120
YDSSSSKEGR TQKEKKAARA RSKGKNSDEE APKTAQKKLK LVRTSPEYGM PSVTFGSVHP 180
SDVLDMPVDP NEPTYCLCHQ VSYGEMIGCD NPDCSIEWFH FACVGLTTKP RGKWFCPRCS 240
QERKKK 246 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
 GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. 
Interpro
 IPR024610; ING_N.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12998; ING
 PF00628; PHD 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS