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Protein

Pantothenate kinase 3

Gene

PANK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921Acetyl-CoA1 Publication
Binding sitei195 – 1951Acetyl-CoA1 Publication
Binding sitei207 – 2071Acetyl-CoA1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Coenzyme A biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.33. 2681.
ReactomeiREACT_11218. Coenzyme A biosynthesis.
UniPathwayiUPA00241; UER00352.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate kinase 3 (EC:2.7.1.33)
Short name:
hPanK3
Alternative name(s):
Pantothenic acid kinase 3
Gene namesi
Name:PANK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:19365. PANK3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134903180.

Polymorphism and mutation databases

BioMutaiPANK3.
DMDMi27805668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Pantothenate kinase 3PRO_0000161804Add
BLAST

Proteomic databases

MaxQBiQ9H999.
PaxDbiQ9H999.
PRIDEiQ9H999.

PTM databases

PhosphoSiteiQ9H999.

Expressioni

Tissue specificityi

Highly expressed in the liver.1 Publication

Gene expression databases

BgeeiQ9H999.
CleanExiHS_PANK3.
ExpressionAtlasiQ9H999. baseline and differential.
GenevestigatoriQ9H999.

Organism-specific databases

HPAiHPA021795.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi122774. 2 interactions.
STRINGi9606.ENSP00000239231.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 185Combined sources
Beta strandi20 – 3112Combined sources
Helixi36 – 5217Combined sources
Beta strandi56 – 583Combined sources
Turni59 – 613Combined sources
Helixi64 – 685Combined sources
Beta strandi70 – 756Combined sources
Beta strandi78 – 8811Combined sources
Helixi89 – 913Combined sources
Helixi92 – 10110Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 1158Combined sources
Helixi118 – 1214Combined sources
Turni122 – 1243Combined sources
Beta strandi132 – 1354Combined sources
Helixi138 – 15215Combined sources
Beta strandi159 – 1646Combined sources
Turni165 – 1673Combined sources
Turni169 – 1713Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi184 – 20118Combined sources
Beta strandi204 – 2129Combined sources
Helixi215 – 22612Combined sources
Helixi231 – 24010Combined sources
Helixi243 – 2453Combined sources
Beta strandi247 – 2493Combined sources
Helixi250 – 2545Combined sources
Helixi259 – 2613Combined sources
Beta strandi267 – 2704Combined sources
Helixi273 – 2764Combined sources
Helixi278 – 2836Combined sources
Helixi286 – 31227Combined sources
Beta strandi317 – 3215Combined sources
Helixi322 – 3243Combined sources
Helixi329 – 34113Combined sources
Turni342 – 3443Combined sources
Beta strandi348 – 3514Combined sources
Turni352 – 3554Combined sources
Helixi357 – 3648Combined sources
Turni365 – 3673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7PX-ray2.05A/B/C/D12-368[»]
3MK6X-ray1.98A/B/C/D12-368[»]
3SMSX-ray2.20A10-370[»]
ProteinModelPortaliQ9H999.
SMRiQ9H999. Positions 12-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H999.

Family & Domainsi

Sequence similaritiesi

Belongs to the type II pantothenate kinase family.Curated

Phylogenomic databases

eggNOGiCOG5146.
GeneTreeiENSGT00390000020719.
HOGENOMiHOG000194690.
HOVERGENiHBG053495.
InParanoidiQ9H999.
KOiK09680.
OMAiYPLLIVN.
OrthoDBiEOG7R2BJR.
PhylomeDBiQ9H999.
TreeFamiTF314866.

Family and domain databases

InterProiIPR004567. Type_II_PanK.
[Graphical view]
PfamiPF03630. Fumble. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00555. panK_eukar. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIKDAKKPS FPWFGMDIGG TLVKLSYFEP IDITAEEEQE EVESLKSIRK
60 70 80 90 100
YLTSNVAYGS TGIRDVHLEL KDLTLFGRRG NLHFIRFPTQ DLPTFIQMGR
110 120 130 140 150
DKNFSTLQTV LCATGGGAYK FEKDFRTIGN LHLHKLDELD CLVKGLLYID
160 170 180 190 200
SVSFNGQAEC YYFANASEPE RCQKMPFNLD DPYPLLVVNI GSGVSILAVH
210 220 230 240 250
SKDNYKRVTG TSLGGGTFLG LCSLLTGCES FEEALEMASK GDSTQADKLV
260 270 280 290 300
RDIYGGDYER FGLPGWAVAS SFGNMIYKEK RESVSKEDLA RATLVTITNN
310 320 330 340 350
IGSVARMCAV NEKINRVVFV GNFLRVNTLS MKLLAYALDY WSKGQLKALF
360 370
LEHEGYFGAV GALLGLPNFS
Length:370
Mass (Da):41,094
Last modified:March 1, 2001 - v1
Checksum:i71EEFA56079F352D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351A → V in BAD97005 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4368.1.
RefSeqiNP_078870.1. NM_024594.3.
UniGeneiHs.388400.
Hs.591729.

Genome annotation databases

EnsembliENST00000239231; ENSP00000239231; ENSG00000120137.
GeneIDi79646.
KEGGihsa:79646.
UCSCiuc003lzz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4368.1.
RefSeqiNP_078870.1. NM_024594.3.
UniGeneiHs.388400.
Hs.591729.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7PX-ray2.05A/B/C/D12-368[»]
3MK6X-ray1.98A/B/C/D12-368[»]
3SMSX-ray2.20A10-370[»]
ProteinModelPortaliQ9H999.
SMRiQ9H999. Positions 12-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122774. 2 interactions.
STRINGi9606.ENSP00000239231.

PTM databases

PhosphoSiteiQ9H999.

Polymorphism and mutation databases

BioMutaiPANK3.
DMDMi27805668.

Proteomic databases

MaxQBiQ9H999.
PaxDbiQ9H999.
PRIDEiQ9H999.

Protocols and materials databases

DNASUi79646.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000239231; ENSP00000239231; ENSG00000120137.
GeneIDi79646.
KEGGihsa:79646.
UCSCiuc003lzz.2. human.

Organism-specific databases

CTDi79646.
GeneCardsiGC05M167975.
HGNCiHGNC:19365. PANK3.
HPAiHPA021795.
MIMi606161. gene.
neXtProtiNX_Q9H999.
PharmGKBiPA134903180.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5146.
GeneTreeiENSGT00390000020719.
HOGENOMiHOG000194690.
HOVERGENiHBG053495.
InParanoidiQ9H999.
KOiK09680.
OMAiYPLLIVN.
OrthoDBiEOG7R2BJR.
PhylomeDBiQ9H999.
TreeFamiTF314866.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00352.
BRENDAi2.7.1.33. 2681.
ReactomeiREACT_11218. Coenzyme A biosynthesis.

Miscellaneous databases

ChiTaRSiPANK3. human.
EvolutionaryTraceiQ9H999.
GenomeRNAii79646.
NextBioi68786.
PROiQ9H999.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H999.
CleanExiHS_PANK3.
ExpressionAtlasiQ9H999. baseline and differential.
GenevestigatoriQ9H999.

Family and domain databases

InterProiIPR004567. Type_II_PanK.
[Graphical view]
PfamiPF03630. Fumble. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00555. panK_eukar. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPANK3_HUMAN
AccessioniPrimary (citable) accession number: Q9H999
Secondary accession number(s): D3DQL1, Q53FJ9, Q7RTX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 118 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.