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Protein

Ketosamine-3-kinase

Gene

FN3KRP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein-bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000141560-MONOMER.
BRENDAi2.7.1.171. 2681.
2.7.1.172. 2681.
ReactomeiR-HSA-163841. Gamma carboxylation, hypusine formation and arylsulfatase activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketosamine-3-kinase (EC:2.7.1.-)
Alternative name(s):
Fructosamine-3-kinase-related protein
Short name:
FN3K-RP
Short name:
FN3K-related protein
Gene namesi
Name:FN3KRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:25700. FN3KRP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720079.

Polymorphism and mutation databases

BioMutaiFN3KRP.
DMDMi47606765.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Ketosamine-3-kinasePRO_0000216339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HA64.
MaxQBiQ9HA64.
PaxDbiQ9HA64.
PeptideAtlasiQ9HA64.
PRIDEiQ9HA64.

2D gel databases

REPRODUCTION-2DPAGEIPI00099986.

PTM databases

iPTMnetiQ9HA64.
PhosphoSiteiQ9HA64.

Expressioni

Tissue specificityi

Expressed in erythrocytes.1 Publication

Gene expression databases

BgeeiQ9HA64.
ExpressionAtlasiQ9HA64. baseline and differential.
GenevisibleiQ9HA64. HS.

Organism-specific databases

HPAiHPA056172.
HPA065831.

Interactioni

Protein-protein interaction databases

BioGridi122797. 10 interactions.
IntActiQ9HA64. 1 interaction.
MINTiMINT-4715634.
STRINGi9606.ENSP00000269373.

Structurei

3D structure databases

ProteinModelPortaliQ9HA64.
SMRiQ9HA64. Positions 38-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the fructosamine kinase family.Curated

Phylogenomic databases

eggNOGiKOG3021. Eukaryota.
COG3001. LUCA.
GeneTreeiENSGT00390000005730.
HOGENOMiHOG000023913.
HOVERGENiHBG005740.
InParanoidiQ9HA64.
KOiK15523.
OMAiAGGCISK.
OrthoDBiEOG7MH0ZF.
PhylomeDBiQ9HA64.
TreeFamiTF313452.

Family and domain databases

InterProiIPR016477. Fructo-/Ketosamine-3-kinase.
IPR011009. Kinase-like_dom.
[Graphical view]
PfamiPF03881. Fructosamin_kin. 1 hit.
[Graphical view]
PIRSFiPIRSF006221. Ketosamine-3-kinase. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HA64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEELLRRELG CSSVRATGHS GGGCISQGRS YDTDQGRVFV KVNPKAEARR
60 70 80 90 100
MFEGEMASLT AILKTNTVKV PKPIKVLDAP GGGSVLVMEH MDMRHLSSHA
110 120 130 140 150
AKLGAQLADL HLDNKKLGEM RLKEAGTVGR GGGQEERPFV ARFGFDVVTC
160 170 180 190 200
CGYLPQVNDW QEDWVVFYAR QRIQPQMDMV EKESGDREAL QLWSALQLKI
210 220 230 240 250
PDLFRDLEII PALLHGDLWG GNVAEDSSGP VIFDPASFYG HSEYELAIAG
260 270 280 290 300
MFGGFSSSFY SAYHGKIPKA PGFEKRLQLY QLFHYLNHWN HFGSGYRGSS

LNIMRNLVK
Length:309
Mass (Da):34,412
Last modified:May 24, 2004 - v2
Checksum:iEE6101C5BB2A7FF3
GO

Sequence cautioni

The sequence CAB66566.1 differs from that shown. Reason: Erroneous termination at position 198. Translated as Leu.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291G → W in CAB66566 (PubMed:11230166).Curated
Sequence conflicti265 – 2651G → C in AAH01458 (PubMed:15489334).Curated
Sequence conflicti278 – 2781Q → R in BAB13992 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571A → V.
Corresponds to variant rs3748811 [ dbSNP | Ensembl ].
VAR_034057

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY360465 mRNA. Translation: AAQ72344.1.
AL136631 mRNA. Translation: CAB66566.1. Sequence problems.
AK022233 mRNA. Translation: BAB13992.1.
BC001458 mRNA. Translation: AAH01458.2.
BC007611 mRNA. Translation: AAH07611.1.
BC014408 mRNA. Translation: AAH14408.1.
CCDSiCCDS11817.1.
RefSeqiNP_078895.2. NM_024619.3.
UniGeneiHs.31431.

Genome annotation databases

EnsembliENST00000269373; ENSP00000269373; ENSG00000141560.
GeneIDi79672.
KEGGihsa:79672.
UCSCiuc002kfu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY360465 mRNA. Translation: AAQ72344.1.
AL136631 mRNA. Translation: CAB66566.1. Sequence problems.
AK022233 mRNA. Translation: BAB13992.1.
BC001458 mRNA. Translation: AAH01458.2.
BC007611 mRNA. Translation: AAH07611.1.
BC014408 mRNA. Translation: AAH14408.1.
CCDSiCCDS11817.1.
RefSeqiNP_078895.2. NM_024619.3.
UniGeneiHs.31431.

3D structure databases

ProteinModelPortaliQ9HA64.
SMRiQ9HA64. Positions 38-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122797. 10 interactions.
IntActiQ9HA64. 1 interaction.
MINTiMINT-4715634.
STRINGi9606.ENSP00000269373.

PTM databases

iPTMnetiQ9HA64.
PhosphoSiteiQ9HA64.

Polymorphism and mutation databases

BioMutaiFN3KRP.
DMDMi47606765.

2D gel databases

REPRODUCTION-2DPAGEIPI00099986.

Proteomic databases

EPDiQ9HA64.
MaxQBiQ9HA64.
PaxDbiQ9HA64.
PeptideAtlasiQ9HA64.
PRIDEiQ9HA64.

Protocols and materials databases

DNASUi79672.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269373; ENSP00000269373; ENSG00000141560.
GeneIDi79672.
KEGGihsa:79672.
UCSCiuc002kfu.4. human.

Organism-specific databases

CTDi79672.
GeneCardsiFN3KRP.
H-InvDBHIX0173719.
HGNCiHGNC:25700. FN3KRP.
HPAiHPA056172.
HPA065831.
MIMi611683. gene.
neXtProtiNX_Q9HA64.
PharmGKBiPA164720079.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3021. Eukaryota.
COG3001. LUCA.
GeneTreeiENSGT00390000005730.
HOGENOMiHOG000023913.
HOVERGENiHBG005740.
InParanoidiQ9HA64.
KOiK15523.
OMAiAGGCISK.
OrthoDBiEOG7MH0ZF.
PhylomeDBiQ9HA64.
TreeFamiTF313452.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000141560-MONOMER.
BRENDAi2.7.1.171. 2681.
2.7.1.172. 2681.
ReactomeiR-HSA-163841. Gamma carboxylation, hypusine formation and arylsulfatase activation.

Miscellaneous databases

ChiTaRSiFN3KRP. human.
GeneWikiiFN3KRP.
GenomeRNAii79672.
NextBioi68903.
PROiQ9HA64.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HA64.
ExpressionAtlasiQ9HA64. baseline and differential.
GenevisibleiQ9HA64. HS.

Family and domain databases

InterProiIPR016477. Fructo-/Ketosamine-3-kinase.
IPR011009. Kinase-like_dom.
[Graphical view]
PfamiPF03881. Fructosamin_kin. 1 hit.
[Graphical view]
PIRSFiPIRSF006221. Ketosamine-3-kinase. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines."
    Collard F., Delpierre G., Stroobant V., Matthijs G., Van Schaftingen E.
    Diabetes 52:2888-2895(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye and Placenta.
  5. "Fructosamine 3-kinase-related protein and deglycation in human erythrocytes."
    Collard F., Wiame E., Bergans N., Fortpied J., Vertommen D., Vanstapel F., Delpierre G., Van Schaftingen E.
    Biochem. J. 382:137-143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKT3K_HUMAN
AccessioniPrimary (citable) accession number: Q9HA64
Secondary accession number(s): Q969F4, Q9H0U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 24, 2004
Last modified: March 16, 2016
This is version 123 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. 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.