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Protein

MKI67 FHA domain-interacting nucleolar phosphoprotein

Gene

NIFK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • negative regulation of phosphatase activity Source: UniProtKB
  • protein complex assembly Source: UniProtKB
  • rRNA metabolic process Source: UniProtKB
  • rRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
MKI67 FHA domain-interacting nucleolar phosphoprotein
Alternative name(s):
Nucleolar phosphoprotein Nopp34
Nucleolar protein interacting with the FHA domain of pKI-67
Short name:
hNIFK
Gene namesi
Name:NIFK
Synonyms:MKI67IP, NOPP34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:17838. NIFK.

Subcellular locationi

GO - Cellular componenti

  • condensed nuclear chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230S → A: Loss of phosphorylation site. 1 Publication1
Mutagenesisi234T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications1
Mutagenesisi235P → A: Reduces phosphorylation at T-234. 1 Publication1
Mutagenesisi238T → A: Loss of phosphorylation site. Abrogates interaction with MKI67. 2 Publications1
Mutagenesisi239P → A: Reduces phosphorylation at T-234 and T-238. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000155438.
PharmGKBiPA38470.

Polymorphism and mutation databases

BioMutaiMKI67IP.
DMDMi71151919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000816292 – 293MKI67 FHA domain-interacting nucleolar phosphoproteinAdd BLAST292

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei145PhosphoserineCombined sources1
Modified residuei218PhosphoserineCombined sources1
Modified residuei223PhosphothreonineCombined sources1
Modified residuei230Phosphoserine1 Publication1
Modified residuei234PhosphothreonineCombined sources2 Publications1
Modified residuei238PhosphothreonineCombined sources1 Publication1
Modified residuei247PhosphoserineCombined sources1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei279PhosphothreonineCombined sources1

Post-translational modificationi

Sequentially phosphorylated on Thr-238, Thr-234 and Ser-230. Thr-234 is phosphorylated only when Thr-238 is phosphorylated. Likewise, phosphorylation at Ser-230 requires that Thr-234 and Thr-238 are phosphorylated. Phosphorylation enhances MKI67 binding.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BYG3.
MaxQBiQ9BYG3.
PaxDbiQ9BYG3.
PeptideAtlasiQ9BYG3.
PRIDEiQ9BYG3.

2D gel databases

SWISS-2DPAGEQ9BYG3.

PTM databases

iPTMnetiQ9BYG3.
PhosphoSitePlusiQ9BYG3.

Expressioni

Gene expression databases

BgeeiENSG00000155438.
CleanExiHS_MKI67IP.
ExpressionAtlasiQ9BYG3. baseline and differential.
GenevisibleiQ9BYG3. HS.

Organism-specific databases

HPAiCAB015382.
CAB075728.
CAB075729.
HPA035735.
HPA035736.

Interactioni

Subunit structurei

Binds to the FHA domain of MKI67; this interaction is enhanced in mitosis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TNIP1Q150253EBI-2561019,EBI-357849

Protein-protein interaction databases

BioGridi124066. 146 interactors.
DIPiDIP-28134N.
IntActiQ9BYG3. 11 interactors.
MINTiMINT-1031770.
STRINGi9606.ENSP00000285814.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi239 – 251Combined sources13
Helixi254 – 257Combined sources4
Beta strandi260 – 265Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AFFNMR-B226-269[»]
ProteinModelPortaliQ9BYG3.
SMRiQ9BYG3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYG3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 123RRMPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 269Interaction with MKI67Add BLAST44

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4208. Eukaryota.
ENOG4111NF9. LUCA.
GeneTreeiENSGT00390000011515.
HOGENOMiHOG000242795.
HOVERGENiHBG057796.
InParanoidiQ9BYG3.
KOiK14838.
OMAiGIDYNFP.
OrthoDBiEOG091G0RMN.
PhylomeDBiQ9BYG3.
TreeFamiTF315137.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR021043. hNIFK_FHA_Ki67_binding.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF12196. hNIFK_binding. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BYG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATFSGPAGP ILSLNPQEDV EFQKEVAQVR KRITQRKKQE QLTPGVVYVR
60 70 80 90 100
HLPNLLDETQ IFSYFSQFGT VTRFRLSRSK RTGNSKGYAF VEFESEDVAK
110 120 130 140 150
IVAETMNNYL FGERLLECHF MPPEKVHKEL FKDWNIPFKQ PSYPSVKRYN
160 170 180 190 200
RNRTLTQKLR MEERFKKKER LLRKKLAKKG IDYDFPSLIL QKTESISKTN
210 220 230 240 250
RQTSTKGQVL RKKKKKVSGT LDTPEKTVDS QGPTPVCTPT FLERRKSQVA
260 270 280 290
ELNDDDKDDE IVFKQPISCV KEEIQETQTP THSRKKRRRS SNQ
Length:293
Mass (Da):34,222
Last modified:June 1, 2001 - v1
Checksum:i9D288ECF2B4CE119
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027182144P → Q.1 PublicationCorresponds to variant rs17852212dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044971 mRNA. Translation: BAB41210.1.
AK291903 mRNA. Translation: BAF84592.1.
AC018737 Genomic DNA. Translation: AAY14830.1.
CH471103 Genomic DNA. Translation: EAW95261.1.
BC012457 mRNA. Translation: AAH12457.1.
BC022990 mRNA. Translation: AAH22990.1.
BC024238 mRNA. Translation: AAH24238.1.
CCDSiCCDS2135.1.
RefSeqiNP_115766.3. NM_032390.4.
UniGeneiHs.367842.

Genome annotation databases

EnsembliENST00000285814; ENSP00000285814; ENSG00000155438.
GeneIDi84365.
KEGGihsa:84365.
UCSCiuc002tnk.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044971 mRNA. Translation: BAB41210.1.
AK291903 mRNA. Translation: BAF84592.1.
AC018737 Genomic DNA. Translation: AAY14830.1.
CH471103 Genomic DNA. Translation: EAW95261.1.
BC012457 mRNA. Translation: AAH12457.1.
BC022990 mRNA. Translation: AAH22990.1.
BC024238 mRNA. Translation: AAH24238.1.
CCDSiCCDS2135.1.
RefSeqiNP_115766.3. NM_032390.4.
UniGeneiHs.367842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AFFNMR-B226-269[»]
ProteinModelPortaliQ9BYG3.
SMRiQ9BYG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124066. 146 interactors.
DIPiDIP-28134N.
IntActiQ9BYG3. 11 interactors.
MINTiMINT-1031770.
STRINGi9606.ENSP00000285814.

PTM databases

iPTMnetiQ9BYG3.
PhosphoSitePlusiQ9BYG3.

Polymorphism and mutation databases

BioMutaiMKI67IP.
DMDMi71151919.

2D gel databases

SWISS-2DPAGEQ9BYG3.

Proteomic databases

EPDiQ9BYG3.
MaxQBiQ9BYG3.
PaxDbiQ9BYG3.
PeptideAtlasiQ9BYG3.
PRIDEiQ9BYG3.

Protocols and materials databases

DNASUi84365.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285814; ENSP00000285814; ENSG00000155438.
GeneIDi84365.
KEGGihsa:84365.
UCSCiuc002tnk.4. human.

Organism-specific databases

CTDi84365.
GeneCardsiNIFK.
HGNCiHGNC:17838. NIFK.
HPAiCAB015382.
CAB075728.
CAB075729.
HPA035735.
HPA035736.
MIMi611970. gene.
neXtProtiNX_Q9BYG3.
OpenTargetsiENSG00000155438.
PharmGKBiPA38470.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4208. Eukaryota.
ENOG4111NF9. LUCA.
GeneTreeiENSGT00390000011515.
HOGENOMiHOG000242795.
HOVERGENiHBG057796.
InParanoidiQ9BYG3.
KOiK14838.
OMAiGIDYNFP.
OrthoDBiEOG091G0RMN.
PhylomeDBiQ9BYG3.
TreeFamiTF315137.

Miscellaneous databases

EvolutionaryTraceiQ9BYG3.
GeneWikiiMKI67IP.
GenomeRNAii84365.
PROiQ9BYG3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000155438.
CleanExiHS_MKI67IP.
ExpressionAtlasiQ9BYG3. baseline and differential.
GenevisibleiQ9BYG3. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR021043. hNIFK_FHA_Ki67_binding.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF12196. hNIFK_binding. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMK67I_HUMAN
AccessioniPrimary (citable) accession number: Q9BYG3
Secondary accession number(s): A8K788, Q8TB66, Q96ED4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.