CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020368
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MKI67 FHA domain-interacting nucleolar phosphoprotein 
Protein Synonyms/Alias
 Nucleolar phosphoprotein Nopp34; Nucleolar protein interacting with the FHA domain of pKI-67; hNIFK 
Gene Name
 MKI67IP 
Gene Synonyms/Alias
 NIFK; NOPP34 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
139KDWNIPFKQPSYPSVubiquitination[1, 2, 3]
158RNRTLTQKLRMEERFubiquitination[1, 3, 4]
179LRKKLAKKGIDYDFPmethylation[5]
179LRKKLAKKGIDYDFPubiquitination[4]
206TNRQTSTKGQVLRKKubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837] 
Functional Description
  
Sequence Annotation
 DOMAIN 45 123 RRM.
 REGION 226 269 Interaction with MKI67.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 218 218 Phosphoserine.
 MOD_RES 223 223 Phosphothreonine.
 MOD_RES 230 230 Phosphoserine.
 MOD_RES 234 234 Phosphothreonine.
 MOD_RES 238 238 Phosphothreonine.
 MOD_RES 247 247 Phosphoserine.
 MOD_RES 279 279 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Chromosome; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 293 AA 
Protein Sequence
MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR HLPNLLDETQ 60
IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK IVAETMNNYL FGERLLECHF 120
MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN RNRTLTQKLR MEERFKKKER LLRKKLAKKG 180
IDYDFPSLIL QKTESISKTN RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT 240
FLERRKSQVA ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ 293 
Gene Ontology
 GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
 GO:0006461; P:protein complex assembly; NAS:UniProtKB.
 GO:0016072; P:rRNA metabolic process; NAS:UniProtKB.
 GO:0009303; P:rRNA transcription; NAS:UniProtKB. 
Interpro
 IPR021043; hNIFK_FHA_Ki67_binding.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF12196; hNIFK_binding
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS