Q9H999 (PANK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pantothenate kinase 3
Short name=hPanK3
EC=2.7.1.33

Alternative name(s):
Pantothenic acid kinase 3

Gene names

Name:

PANK3

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	370 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	coenzyme A biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantothenate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 370

370

Pantothenate kinase 3

PRO_0000161804

Sites

Binding site

192

1

Acetyl-CoA

Binding site

195

1

Acetyl-CoA

Binding site

207

1

Acetyl-CoA

Experimental info

Sequence conflict

335

1

A → V in BAD97005. Ref.2

Secondary structure

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370

Helix Strand Turn

Details...

Beta strand

14 – 18

5

Beta strand

20 – 31

12

Helix

36 – 52

17

Beta strand

56 – 58

3

Turn

59 – 61

3

Helix

64 – 68

5

Beta strand

70 – 75

6

Beta strand

78 – 88

11

Helix

89 – 91

3

Helix

92 – 101

10

Helix

105 – 107

3

Beta strand

108 – 115

8

Helix

118 – 121

4

Turn

122 – 124

3

Beta strand

132 – 135

4

Helix

138 – 152

15

Beta strand

159 – 164

6

Turn

165 – 167

3

Turn

169 – 171

3

Beta strand

173 – 176

4

Beta strand

184 – 201

18

Beta strand

204 – 212

9

Helix

215 – 226

12

Helix

231 – 240

10

Helix

243 – 245

3

Beta strand

247 – 249

3

Helix

250 – 254

5

Helix

259 – 261

3

Beta strand

267 – 270

4

Helix

273 – 276

4

Helix

278 – 283

6

Helix

286 – 312

27

Beta strand

317 – 321

5

Helix

322 – 324

3

Helix

329 – 341

13

Turn

342 – 344

3

Beta strand

348 – 351

4

Turn

352 – 355

4

Helix

357 – 364

8

Turn

365 – 367

3

Sequences

	Sequence		Length	Mass (Da)
	Q9H999 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 71EEFA56079F352D	FASTA	370	41,094
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00178232.

RefSeq

NP_078870.1. NM_024594.3.

UniGene

Hs.388400.
Hs.591729.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I7P	X-ray	2.05	A/B/C/D	12-368	[»]
3MK6	X-ray	1.98	A/B/C/D	12-368	[»]
3SMS	X-ray	2.20	A	10-370	[»]

ProteinModelPortal

Q9H999.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000239231.

PTM databases

PhosphoSite

Q9H999.

Polymorphism databases

DMDM

27805668.

Proteomic databases

PaxDb

Q9H999.

PRIDE

Q9H999.

Protocols and materials databases

DNASU

79646.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000239231; ENSP00000239231; ENSG00000120137.

GeneID

79646.

KEGG

hsa:79646.

UCSC

uc003lzz.2. human.

Organism-specific databases

CTD

79646.

GeneCards

GC05M167975.

HGNC

HGNC:19365. PANK3.

HPA

HPA021795.

MIM

606161. gene.

neXtProt

NX_Q9H999.

PharmGKB

PA134903180.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5146.

HOGENOM

HOG000194690.

HOVERGEN

HBG053495.

InParanoid

Q9H999.

KO

K09680.

OMA

HDLPTFI.

OrthoDB

EOG4PZJ6Z.

PhylomeDB

Q9H999.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00241; UER00352.

Gene expression databases

ArrayExpress

Q9H999.

Bgee

Q9H999.

CleanEx

HS_PANK3.

Genevestigator

Q9H999.

GermOnline

ENSG00000120137. Homo sapiens.

Family and domain databases

InterPro

IPR004567. Type_II_PanK.
[Graphical view]

Pfam

PF03630. Fumble. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00555. panK_eukar. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

PANK3. human.

EvolutionaryTrace

Q9H999.

GenomeRNAi

79646.

NextBio

68786.

SOURCE

Search...

Entry information

Entry name

PANK3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 1 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.