CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000388
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Mdm4 
Protein Synonyms/Alias
 Double minute 4 protein; Mdm2-like p53-binding protein; Protein Mdmx; p53-binding protein Mdm4 
Gene Name
 MDM4 
Gene Synonyms/Alias
 MDMX 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
328FRCWALRKDWYSDCSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. 
Sequence Annotation
 DOMAIN 26 106 SWIB.
 ZN_FING 300 329 RanBP2-type.
 ZN_FING 437 478 RING-type.
 REGION 246 332 Region II.
 REGION 393 490 Necessary for interaction with UBP2.
 MOTIF 442 445 Nuclear localization signal (Potential).
 MOD_RES 342 342 Phosphoserine; by CHEK2.
 MOD_RES 367 367 Phosphoserine; by CHEK1 and CHEK2.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 490 AA 
Protein Sequence
MTSFSTSAQC STSDSACRIS PGQINQVRPK LPLLKILHAA GAQGEMFTVK EVMHYLGQYI 60
MVKQLYDQQE QHMVYCGGDL LGELLGRQSF SVKDPSPLYD MLRKNLVTLA TATTDAAQTL 120
ALAQDHSMDI PSQDQLKQSA EESSTSRKRT TEDDIPTLPT SEHKCIHSRE DEDLIENLAQ 180
DETSRLDLGF EEWDVAGLPW WFLGNLRSNY TPRSNGSTDL QTNQDVGTAI VSDTTDDLWF 240
LNESVSEQLG VGIKVEAADT EQTSEEVGKV SDKKVIEVGK NDDLEDSKSL SDDTDVEVTS 300
EDEWQCTECK KFNSPSKRYC FRCWALRKDW YSDCSKLTHS LSTSDITAIP EKENEGNDVP 360
DCRRTISAPV VRPKDAYIKK ENSKLFDPCN SVEFLDLAHS SESQETISSM GEQLDNLSEQ 420
RTDTENMEDC QNLLKPCSLC EKRPRDGNII HGRTGHLVTC FHCARRLKKA GASCPICKKE 480
IQLVIKVFIA 490 
Gene Ontology
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; TAS:UniProtKB.
 GO:0008283; P:cell proliferation; IEP:UniProtKB.
 GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
 GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEP:UniProtKB.
 GO:0045023; P:G0 to G1 transition; IEP:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
 GO:0071157; P:negative regulation of cell cycle arrest; IEA:InterPro.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0006461; P:protein complex assembly; IDA:UniProtKB.
 GO:0050821; P:protein stabilization; IEP:UniProtKB. 
Interpro
 IPR015458; MDM4.
 IPR016495; p53_neg-reg_MDM_2/4.
 IPR003121; SWIB_MDM2_domain.
 IPR001876; Znf_RanBP2.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02201; SWIB
 PF00641; zf-RanBP 
SMART
 SM00184; RING
 SM00547; ZnF_RBZ 
PROSITE
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS