Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  MKI67 FHA domain-interacting nucleolar phosphoprotein  

UniProtKB / Swiss-Prot ID :  MK67I_HUMAN

Gene Name (Synonyms) : 
MKI67IP, NIFK, NOPP34  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleolus. Chromosome. Note=Localizes to mitotic chromosomes in conjunction with MKI67. 

Protein Function :   

Protein Sequence MATFSGPAGPILSLNPQEDVEFQKEVAQVRKRITQRKKQEQLTPGVVYVRHLPNLLDETQIFSYFSQFGT...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHCCCCCHHHHHHHHCCCCCCCCCCCCCEEEEECCCCCCCHHHHHHHHHHCCC...
Protein Variant
LocationDescription
144P -> Q (in dbSNP:rs17852212). VAR_027182
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATFSG
---CCCCCC
19.83UniProtKB
Link-
139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NIPFKQPSY
CCCCCCCCC
56.81Phosphositeplus
Link-
158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TLTQKLRME
HHHHHHHHH
32.59Phosphositeplus
Link-
183PhosphotyrosineKGIDYDFPS
CCCCCCCCC
19.98Phosphositeplus
Link-
218PhosphoserineKKKVSGTLD
CHHHCCCCC
34.63HPRD
Link-
218PhosphoserineKKKVSGTLD
CHHHCCCCC
34.63PhosphoELM
Link-
218PhosphoserineKKKVSGTLD
CHHHCCCCC
34.63Phosphositeplus
Link-
218Phosphoserine.KKKVSGTLD
CHHHCCCCC
34.63UniProtKB
Link-
220PhosphothreonineKVSGTLDTP
HHCCCCCCC
17.60HPRD
Link-
220PhosphothreonineKVSGTLDTP
HHCCCCCCC
17.60PhosphoELM
Link-
220PhosphothreonineKVSGTLDTP
HHCCCCCCC
17.60Phosphositeplus
Link-
220Phosphothreonine.KVSGTLDTP
HHCCCCCCC
17.60UniProtKB
Link-
223PhosphothreonineGTLDTPEKT
CCCCCCCCE
36.14HPRD
Link-
223PhosphothreonineGTLDTPEKT
CCCCCCCCE
36.14PhosphoELM
Link-
223PhosphothreonineGTLDTPEKT
CCCCCCCCE
36.14Phosphositeplus
Link-
223PhosphothreonineGTLDTPEKT
CCCCCCCCE
36.14SysPTM
Link-
223Phosphothreonine.GTLDTPEKT
CCCCCCCCE
36.14UniProtKB
Link-
227PhosphothreonineTPEKTVDSQ
CCCCEEECC
28.08HPRD
Link
227PhosphothreonineTPEKTVDSQ
CCCCEEECC
28.08PhosphoELM
Link
227PhosphothreonineTPEKTVDSQ
CCCCEEECC
28.08Phosphositeplus
Link
230PhosphoserineKTVDSQGPT
CEEECCCCC
32.47HPRD
Link
230PhosphoserineKTVDSQGPT
CEEECCCCC
32.47Phosphositeplus
Link
230Phosphoserine (GSK-3_alpha;GSK-3_beta)KTVDSQGPT
CEEECCCCC
32.47PhosphoELM
Link
230Phosphoserine.KTVDSQGPT
CEEECCCCC
32.47UniProtKB
Link
234PhosphothreonineSQGPTPVCT
CCCCCCCCC
34.87HPRD
Link
234PhosphothreonineSQGPTPVCT
CCCCCCCCC
34.87Phosphositeplus
Link
234PhosphothreonineSQGPTPVCT
CCCCCCCCC
34.87SysPTM
Link
234Phosphothreonine (GSK-3_alpha;GSK-3_beta)SQGPTPVCT
CCCCCCCCC
34.87PhosphoELM
Link
234Phosphothreonine.SQGPTPVCT
CCCCCCCCC
34.87UniProtKB
Link
238PhosphothreonineTPVCTPTFL
CCCCCCCEE
26.12HPRD
Link
238PhosphothreonineTPVCTPTFL
CCCCCCCEE
26.12PhosphoELM
Link
238PhosphothreonineTPVCTPTFL
CCCCCCCEE
26.12Phosphositeplus
Link
238PhosphothreonineTPVCTPTFL
CCCCCCCEE
26.12SysPTM
Link
238Phosphothreonine.TPVCTPTFL
CCCCCCCEE
26.12UniProtKB
Link
240PhosphothreonineVCTPTFLER
CCCCCEEEC
23.77HPRD
Link
240PhosphothreonineVCTPTFLER
CCCCCEEEC
23.77PhosphoELM
Link
240PhosphothreonineVCTPTFLER
CCCCCEEEC
23.77Phosphositeplus
Link
240Phosphothreonine.VCTPTFLER
CCCCCEEEC
23.77UniProtKB
Link
247PhosphoserineERRKSQVAE
ECCCCEEEE
28.24HPRD
Link
247PhosphoserineERRKSQVAE
ECCCCEEEE
28.24PhosphoELM
Link
247PhosphoserineERRKSQVAE
ECCCCEEEE
28.24Phosphositeplus
Link
247PhosphoserineERRKSQVAE
ECCCCEEEE
28.24SysPTM
Link
247Phosphoserine.ERRKSQVAE
ECCCCEEEE
28.24UniProtKB
Link
279PhosphothreonineQETQTPTHS
CCCCCCHHH
37.26HPRD
Link-
279PhosphothreonineQETQTPTHS
CCCCCCHHH
37.26PhosphoELM
Link-
279PhosphothreonineQETQTPTHS
CCCCCCHHH
37.26Phosphositeplus
Link-
279PhosphothreonineQETQTPTHS
CCCCCCHHH
37.26SysPTM
Link-
279Phosphothreonine.QETQTPTHS
CCCCCCHHH
37.26UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
KI67_HUMANphysical interaction
physical interaction
physical interaction
DIP:56662EDIP11342549
11342549
11342549
MK67I_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:17576HPRD11342549
KI67_HUMANin vitro
yeast 2-hybrid
HPRD:17576HPRD11342549
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-223; THR-234 AND THR-238, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-240 ANDSER-247, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; THR-220; THR-223;SER-230; THR-234; SER-247 AND THR-279, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234; THR-238; SER-247AND THR-279, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-223; THR-234 AND THR-238, AND MASSSPECTROMETRY.
"Sequential phosphorylation and multisite interactions characterizespecific target recognition by the FHA domain of Ki67.";
Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.;
Nat. Struct. Mol. Biol. 12:987-993(2005).
Cited for: STRUCTURE BY NMR OF 226-269 IN COMPLEX WITH MKI67, MASS SPECTROMETRY,MUTAGENESIS OF SER-230; THR-234; PRO-235; THR-238 AND PRO-239, ANDPHOSPHORYLATION AT SER-230; THR-234 AND THR-238.
"Structure of human Ki67 FHA domain and its binding to aphosphoprotein fragment from hNIFK reveal unique recognition sites andnew views to the structural basis of FHA domain functions.";
Li H., Byeon I.-J., Ju Y., Tsai M.-D.;
J. Mol. Biol. 335:371-381(2004).
Cited for: PHOSPHORYLATION AT THR-234, AND INTERACTION WITH MKI67.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures