Q9UHJ6 (SHPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sedoheptulokinase
Short name=SHK
EC=2.7.1.14

Alternative name(s):
Carbohydrate kinase-like protein

Gene names

Name:	SHPK
Synonyms:	CARKL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a modulator of macrophage activation through control of glucose metabolism By similarity.
Catalytic activity	ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate. Ref.7
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Strongly expressed in liver, kidney and pancreas. Expressed at lower levels in placenta and heart. Very weakly expressed in lung and brain. Ref.1
Induction	Down-regulated by LPS. Ref.9
Sequence similarities	Belongs to the FGGY kinase family.
Biophysicochemical properties	Kinetic parameters: KM=0.06 mM for sedoheptulose Ref.7 pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interleukin-13 Inferred from sequence or structural similarity. Source: UniProtKB cellular response to interleukin-4 Inferred from sequence or structural similarity. Source: UniProtKB cellular response to lipopolysaccharide Inferred from direct assay Ref.9. Source: UniProtKB pentose-phosphate shunt, non-oxidative branch Inferred from sequence or structural similarity. Source: UniProtKB regulation of inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB regulation of macrophage activation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW sedoheptulokinase activity Inferred from direct assay PubMed 19413330. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	Sedoheptulokinase		PRO_0000059564
Natural variations
	Natural variant	215	1	E → K. Ref.1 Corresponds to variant rs150857 [ dbSNP | Ensembl ].		VAR_042580
	Natural variant	421	1	D → E. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Corresponds to variant rs224496 [ dbSNP | Ensembl ].		VAR_048591
	Natural variant	434	1	L → M. Corresponds to variant rs36125540 [ dbSNP | Ensembl ].		VAR_048592

Sequences

	Sequence		Length	Mass (Da)
	Q9UHJ6 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 0C920A380927AC1E	FASTA	478	51,491
	10 20 30 40 50 60 MAARPITLGI DLGTTSVKAA LLRAAPDDPS GFAVLASCAR AARAEAAVES AVAGPQGREQ 70 80 90 100 110 120 DVSRILQALH ECLAALPRPQ LRSVVGIGVS GQMHGVVFWK TGQGCEWTEG GITPVFEPRA 130 140 150 160 170 180 VSHLVTWQDG RCSSEFLASL PQPKSHLSVA TGFGCATIFW LLKYRPEFLK SYDAAGTIHD 190 200 210 220 230 240 YVVAMLCGLP RPLMSDQNAA SWGYFNTQSQ SWNVETLRSS GFPVHLLPDI AEPGSVAGRT 250 260 270 280 290 300 SHMWFEIPKG TQVGVALGDL QASVYSCMAQ RTDAVLNIST SVQLAASMPS GFQPAQTPDP 310 320 330 340 350 360 TAPVAYFPYF NRTYLGVAAS LNGGNVLATF VHMLVQWMAD LGLEVEESTV YSRMIQAAVQ 370 380 390 400 410 420 QRDTHLTITP TVLGERHLPD QLASVTRISS SDLSLGHVTR ALCRGIVQNL HSMLPIQQLQ 430 440 450 460 470 DWGVERVMGS GSALSRNDVL KQEVQRAFPL PMSFGQDVDA AVGAALVMLR RHLNQKES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion." Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G., Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A., Green E.D. Genome Res. 10:165-173(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS LYS-215 AND GLU-421. Tissue: Fetal kidney.
[2]	"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], VARIANT GLU-421. Tissue: Brain.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-421. Tissue: Melanoma.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-421.
[6]	"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], VARIANT GLU-421. Tissue: Liver.
[7]	"Sedoheptulokinase deficiency due to a 57-kb deletion in cystinosis patients causes urinary accumulation of sedoheptulose: elucidation of the CARKL gene." Wamelink M.M., Struys E.A., Jansen E.E., Levtchenko E.N., Zijlstra F.S., Engelke U., Blom H.J., Jakobs C., Wevers R.A. Hum. Mutat. 29:532-536(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"The sedoheptulose kinase CARKL directs macrophage polarization through control of glucose metabolism." Haschemi A., Kosma P., Gille L., Evans C.R., Burant C.F., Starkl P., Knapp B., Haas R., Schmid J.A., Jandl C., Amir S., Lubec G., Park J., Esterbauer H., Bilban M., Brizuela L., Pospisilik J.A., Otterbein L.E., Wagner O. Cell Metab. 15:813-826(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF163573 mRNA. Translation: AAF24936.1. AF168787 Genomic DNA. Translation: AAF43103.1. AK312428 mRNA. Translation: BAG35337.1. AL832420 mRNA. Translation: CAH10646.1. AC027796 Genomic DNA. No translation available. CH471108 Genomic DNA. Translation: EAW90501.1. BC020543 mRNA. Translation: AAH20543.1.
IPI	IPI00005914.
RefSeq	NP_037408.2. NM_013276.2.
UniGene	Hs.579217.
3D structure databases
ProteinModelPortal	Q9UHJ6.
SMR	Q9UHJ6. Positions 8-374.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UHJ6. 1 interaction.
STRING	9606.ENSP00000225519.
PTM databases
PhosphoSite	Q9UHJ6.
Polymorphism databases
DMDM	296452959.
Proteomic databases
PaxDb	Q9UHJ6.
PRIDE	Q9UHJ6.
Protocols and materials databases
DNASU	23729.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000225519; ENSP00000225519; ENSG00000197417.
GeneID	23729.
KEGG	hsa:23729.
UCSC	uc002fvz.1. human.
Organism-specific databases
CTD	23729.
GeneCards	GC17M003514.
HGNC	HGNC:1492. SHPK.
HPA	HPA024361.
MIM	605060. gene.
neXtProt	NX_Q9UHJ6.
PharmGKB	PA162403312.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1070.
HOGENOM	HOG000008078.
HOVERGEN	HBG050796.
InParanoid	Q9UHJ6.
KO	K11214.
OMA	FQCSVYS.
OrthoDB	EOG4FR0RN.
PhylomeDB	Q9UHJ6.
Gene expression databases
Bgee	Q9UHJ6.
CleanEx	HS_SHPK.
Genevestigator	Q9UHJ6.
GermOnline	ENSG00000197417. Homo sapiens.
Family and domain databases
InterPro	IPR018484. Carb_kinase_FGGY_N. [Graphical view]
Pfam	PF00370. FGGY_N. 1 hit. [Graphical view]
PROSITE	PS00933. FGGY_KINASES_1. False negative. PS00445. FGGY_KINASES_2. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23729.
NextBio	46633.
SOURCE	Search...

Entry information

Entry name

SHPK_HUMAN

Accession

Primary (citable) accession number: Q9UHJ6
Secondary accession number(s): B2R640, Q8WUH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.