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Q9UHJ6

- SHPK_HUMAN

UniProt

Q9UHJ6 - SHPK_HUMAN

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Protein

Sedoheptulokinase

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

Functioni

Acts as a modulator of macrophage activation through control of glucose metabolism By similarity.

Catalytic activityi

ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate.1 Publication

Kineticsi

  1. KM=0.06 mM for sedoheptulose1 Publication

pH dependencei

Optimum pH is 8.5.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. sedoheptulokinase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB
  2. cellular response to interleukin-13 Source: UniProtKB
  3. cellular response to interleukin-4 Source: UniProtKB
  4. cellular response to lipopolysaccharide Source: UniProtKB
  5. pentose-phosphate shunt, non-oxidative branch Source: UniProtKB
  6. phosphorylation Source: UniProtKB
  7. regulation of inflammatory response Source: UniProtKB
  8. regulation of macrophage activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sedoheptulokinase (EC:2.7.1.14)
Short name:
SHK
Alternative name(s):
Carbohydrate kinase-like protein
Gene namesi
Name:SHPK
Synonyms:CARKL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1492. SHPK.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162403312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 478477SedoheptulokinasePRO_0000059564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UHJ6.
PaxDbiQ9UHJ6.
PRIDEiQ9UHJ6.

PTM databases

PhosphoSiteiQ9UHJ6.

Expressioni

Tissue specificityi

Strongly expressed in liver, kidney and pancreas. Expressed at lower levels in placenta and heart. Very weakly expressed in lung and brain.1 Publication

Inductioni

Down-regulated by LPS.1 Publication

Gene expression databases

BgeeiQ9UHJ6.
CleanExiHS_SHPK.
GenevestigatoriQ9UHJ6.

Organism-specific databases

HPAiHPA024361.

Interactioni

Protein-protein interaction databases

BioGridi117235. 2 interactions.
IntActiQ9UHJ6. 1 interaction.
STRINGi9606.ENSP00000225519.

Structurei

3D structure databases

ProteinModelPortaliQ9UHJ6.
SMRiQ9UHJ6. Positions 8-374.

Family & Domainsi

Sequence similaritiesi

Belongs to the FGGY kinase family.

Phylogenomic databases

eggNOGiCOG1070.
HOGENOMiHOG000008078.
HOVERGENiHBG050796.
InParanoidiQ9UHJ6.
KOiK11214.
OMAiFQCSVYS.
PhylomeDBiQ9UHJ6.
TreeFamiTF315140.

Family and domain databases

InterProiIPR018484. Carb_kinase_FGGY_N.
IPR028491. Sedoheptulokinase.
[Graphical view]
PANTHERiPTHR10196:SF22. PTHR10196:SF22. 1 hit.
PfamiPF00370. FGGY_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UHJ6-1 [UniParc]FASTAAdd to Basket

« Hide

MAARPITLGI DLGTTSVKAA LLRAAPDDPS GFAVLASCAR AARAEAAVES    50
AVAGPQGREQ DVSRILQALH ECLAALPRPQ LRSVVGIGVS GQMHGVVFWK 100
TGQGCEWTEG GITPVFEPRA VSHLVTWQDG RCSSEFLASL PQPKSHLSVA 150
TGFGCATIFW LLKYRPEFLK SYDAAGTIHD YVVAMLCGLP RPLMSDQNAA 200
SWGYFNTQSQ SWNVETLRSS GFPVHLLPDI AEPGSVAGRT SHMWFEIPKG 250
TQVGVALGDL QASVYSCMAQ RTDAVLNIST SVQLAASMPS GFQPAQTPDP 300
TAPVAYFPYF NRTYLGVAAS LNGGNVLATF VHMLVQWMAD LGLEVEESTV 350
YSRMIQAAVQ QRDTHLTITP TVLGERHLPD QLASVTRISS SDLSLGHVTR 400
ALCRGIVQNL HSMLPIQQLQ DWGVERVMGS GSALSRNDVL KQEVQRAFPL 450
PMSFGQDVDA AVGAALVMLR RHLNQKES 478
Length:478
Mass (Da):51,491
Last modified:May 18, 2010 - v3
Checksum:i0C920A380927AC1E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151E → K.1 Publication
Corresponds to variant rs150857 [ dbSNP | Ensembl ].
VAR_042580
Natural varianti421 – 4211D → E.5 Publications
Corresponds to variant rs224496 [ dbSNP | Ensembl ].
VAR_048591
Natural varianti434 – 4341L → M.
Corresponds to variant rs36125540 [ dbSNP | Ensembl ].
VAR_048592

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11030.1.
RefSeqiNP_037408.2. NM_013276.2.
UniGeneiHs.579217.

Genome annotation databases

EnsembliENST00000225519; ENSP00000225519; ENSG00000197417.
GeneIDi23729.
KEGGihsa:23729.
UCSCiuc002fvz.1. human.

Polymorphism databases

DMDMi296452959.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11030.1.
RefSeqi NP_037408.2. NM_013276.2.
UniGenei Hs.579217.

3D structure databases

ProteinModelPortali Q9UHJ6.
SMRi Q9UHJ6. Positions 8-374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117235. 2 interactions.
IntActi Q9UHJ6. 1 interaction.
STRINGi 9606.ENSP00000225519.

PTM databases

PhosphoSitei Q9UHJ6.

Polymorphism databases

DMDMi 296452959.

Proteomic databases

MaxQBi Q9UHJ6.
PaxDbi Q9UHJ6.
PRIDEi Q9UHJ6.

Protocols and materials databases

DNASUi 23729.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225519 ; ENSP00000225519 ; ENSG00000197417 .
GeneIDi 23729.
KEGGi hsa:23729.
UCSCi uc002fvz.1. human.

Organism-specific databases

CTDi 23729.
GeneCardsi GC17M003514.
HGNCi HGNC:1492. SHPK.
HPAi HPA024361.
MIMi 605060. gene.
neXtProti NX_Q9UHJ6.
PharmGKBi PA162403312.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1070.
HOGENOMi HOG000008078.
HOVERGENi HBG050796.
InParanoidi Q9UHJ6.
KOi K11214.
OMAi FQCSVYS.
PhylomeDBi Q9UHJ6.
TreeFami TF315140.

Miscellaneous databases

GenomeRNAii 23729.
NextBioi 46633.
PROi Q9UHJ6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHJ6.
CleanExi HS_SHPK.
Genevestigatori Q9UHJ6.

Family and domain databases

InterProi IPR018484. Carb_kinase_FGGY_N.
IPR028491. Sedoheptulokinase.
[Graphical view ]
PANTHERi PTHR10196:SF22. PTHR10196:SF22. 1 hit.
Pfami PF00370. FGGY_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: INDUCTION.

Entry informationi

Entry nameiSHPK_HUMAN
AccessioniPrimary (citable) accession number: Q9UHJ6
Secondary accession number(s): B2R640, Q8WUH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 109 of the entry and version 3 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

External Data

Dasty 3

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