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Q9H999 (PANK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate kinase 3

Short name=hPanK3
EC=2.7.1.33
Alternative name(s):
Pantothenic acid kinase 3
Gene names
Name:PANK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the physiological regulation of the intracellular CoA concentration By similarity.

Catalytic activity

ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate.

Enzyme regulation

Regulated by feedback inhibition by CoA and its thioesters By similarity.

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.

Subunit structure

Homodimer. Ref.6

Subcellular location

Cytoplasm Probable.

Tissue specificity

Highly expressed in the liver. Ref.5

Sequence similarities

Belongs to the type II pantothenate kinase family.

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcoenzyme A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantothenate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Pantothenate kinase 3
PRO_0000161804

Sites

Binding site1921Acetyl-CoA
Binding site1951Acetyl-CoA
Binding site2071Acetyl-CoA

Experimental info

Sequence conflict3351A → V in BAD97005. Ref.2

Secondary structure

...................................................................... 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H999 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 71EEFA56079F352D

FASTA37041,094
        10         20         30         40         50         60 
MKIKDAKKPS FPWFGMDIGG TLVKLSYFEP IDITAEEEQE EVESLKSIRK YLTSNVAYGS 

        70         80         90        100        110        120 
TGIRDVHLEL KDLTLFGRRG NLHFIRFPTQ DLPTFIQMGR DKNFSTLQTV LCATGGGAYK 

       130        140        150        160        170        180 
FEKDFRTIGN LHLHKLDELD CLVKGLLYID SVSFNGQAEC YYFANASEPE RCQKMPFNLD 

       190        200        210        220        230        240 
DPYPLLVVNI GSGVSILAVH SKDNYKRVTG TSLGGGTFLG LCSLLTGCES FEEALEMASK 

       250        260        270        280        290        300 
GDSTQADKLV RDIYGGDYER FGLPGWAVAS SFGNMIYKEK RESVSKEDLA RATLVTITNN 

       310        320        330        340        350        360 
IGSVARMCAV NEKINRVVFV GNFLRVNTLS MKLLAYALDY WSKGQLKALF LEHEGYFGAV 

       370 
GALLGLPNFS 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovium.
[3]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. expand/collapse author list , 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].
[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: Lymph.
[5]"A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome."
Zhou B., Westaway S.K., Levinson B., Johnson M.A., Gitschier J., Hayflick S.J.
Nat. Genet. 28:345-349(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder."
Hong B.S., Senisterra G., Rabeh W.M., Vedadi M., Leonardi R., Zhang Y.M., Rock C.O., Jackowski S., Park H.W.
J. Biol. Chem. 282:27984-27993(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 12-368 IN COMPLEX WITH ACETYL-COA, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022961 mRNA. Translation: BAB14333.1.
AK223285 mRNA. Translation: BAD97005.1.
CH471062 Genomic DNA. Translation: EAW61503.1.
CH471062 Genomic DNA. Translation: EAW61505.1.
BC013705 mRNA. Translation: AAH13705.1.
BK000011 mRNA. Translation: DAA00005.1.
CCDSCCDS4368.1.
RefSeqNP_078870.1. NM_024594.3.
UniGeneHs.388400.
Hs.591729.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7PX-ray2.05A/B/C/D12-368[»]
3MK6X-ray1.98A/B/C/D12-368[»]
3SMSX-ray2.20A10-370[»]
ProteinModelPortalQ9H999.
SMRQ9H999. Positions 12-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122774. 2 interactions.
STRING9606.ENSP00000239231.

PTM databases

PhosphoSiteQ9H999.

Polymorphism databases

DMDM27805668.

Proteomic databases

MaxQBQ9H999.
PaxDbQ9H999.
PRIDEQ9H999.

Protocols and materials databases

DNASU79646.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000239231; ENSP00000239231; ENSG00000120137.
GeneID79646.
KEGGhsa:79646.
UCSCuc003lzz.2. human.

Organism-specific databases

CTD79646.
GeneCardsGC05M167975.
HGNCHGNC:19365. PANK3.
HPAHPA021795.
MIM606161. gene.
neXtProtNX_Q9H999.
PharmGKBPA134903180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5146.
HOGENOMHOG000194690.
HOVERGENHBG053495.
InParanoidQ9H999.
KOK09680.
OMAYPLLIVN.
OrthoDBEOG7R2BJR.
PhylomeDBQ9H999.
TreeFamTF314866.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00241; UER00352.

Gene expression databases

ArrayExpressQ9H999.
BgeeQ9H999.
CleanExHS_PANK3.
GenevestigatorQ9H999.

Family and domain databases

InterProIPR004567. Type_II_PanK.
[Graphical view]
PfamPF03630. Fumble. 1 hit.
[Graphical view]
TIGRFAMsTIGR00555. panK_eukar. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPANK3. human.
EvolutionaryTraceQ9H999.
GenomeRNAi79646.
NextBio68786.
PROQ9H999.
SOURCESearch...

Entry information

Entry namePANK3_HUMAN
AccessionPrimary (citable) accession number: Q9H999
Secondary accession number(s): D3DQL1, Q53FJ9, Q7RTX4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM