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Protein

Pantothenate kinase 2, mitochondrial

Gene

PANK2

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

Functioni

May be the master regulator of the CoA biosynthesis.By similarity

Catalytic activityi

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

Enzyme regulationi

Regulated by feedback inhibition by CoA and its thioesters.

Pathway:icoenzyme A biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CoA from (R)-pantothenate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Pantothenate kinase 4 (PANK4), Pantothenate kinase 3 (PANK3), Pantothenate kinase 1 (PANK1), Pantothenate kinase 2, mitochondrial (PANK2)
  2. Phosphopantothenate--cysteine ligase (PPCS)
  3. Phosphopantothenoylcysteine decarboxylase (PPCDC)
  4. Bifunctional coenzyme A synthase (COASY)
  5. Bifunctional coenzyme A synthase (COASY)
This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei392 – 3921Acetyl-CoABy similarity
Binding sitei395 – 3951Acetyl-CoABy similarity
Binding sitei407 – 4071Acetyl-CoABy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • pantothenate kinase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • aerobic respiration Source: Ensembl
  • coenzyme A biosynthetic process Source: ParkinsonsUK-UCL
  • coenzyme biosynthetic process Source: Reactome
  • mitochondrion morphogenesis Source: Ensembl
  • pantothenate metabolic process Source: ParkinsonsUK-UCL
  • phosphorylation Source: ParkinsonsUK-UCL
  • regulation of bile acid metabolic process Source: ParkinsonsUK-UCL
  • regulation of fatty acid metabolic process Source: ParkinsonsUK-UCL
  • regulation of mitochondrial membrane potential Source: Ensembl
  • regulation of triglyceride metabolic process Source: ParkinsonsUK-UCL
  • small molecule metabolic process Source: Reactome
  • spermatid development Source: Ensembl
  • vitamin metabolic process Source: Reactome
  • water-soluble vitamin metabolic process Source: Reactome
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.
SABIO-RKQ9BZ23.
UniPathwayiUPA00241; UER00352.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate kinase 2, mitochondrial (EC:2.7.1.33)
Short name:
hPanK2
Alternative name(s):
Pantothenic acid kinase 2
Gene namesi
Name:PANK2
Synonyms:C20orf48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15894. PANK2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrion Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Neurodegeneration with brain iron accumulation 1 (NBIA1)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. Clinical manifestations include progressive muscle spasticity, hyperreflexia, muscle rigidity, dystonia, dysarthria, and intellectual deterioration which progresses to severe dementia over several years. It is clinically classified into classic, atypical, and intermediate phenotypes. Classic forms present with onset in first decade, rapid progression, loss of independent ambulation within 15 years. Atypical forms have onset in second decade, slow progression, maintenance of independent ambulation up to 40 years later. Intermediate forms manifest onset in first decade with slow progression or onset in second decade with rapid progression. Patients with early onset tend to also develop pigmentary retinopathy, whereas those with later onset tend to also have speech disorders and psychiatric features. All patients have the 'eye of the tiger' sign on brain MRI.

See also OMIM:234200
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341E → G in NBIA1. 1 Publication
VAR_060934
Natural varianti219 – 2191G → V in NBIA1; atypical. 1 Publication
VAR_015154
Natural varianti234 – 2341T → A in NBIA1; atypical. 1 Publication
VAR_015155
Natural varianti249 – 2491R → P in NBIA1. 1 Publication
VAR_060935
Natural varianti264 – 2641R → W in NBIA1. 1 Publication
VAR_015156
Natural varianti278 – 2781R → C in NBIA1; atypical. 1 Publication
VAR_015157
Natural varianti278 – 2781R → L in NBIA1. 1 Publication
VAR_060936
Natural varianti282 – 2821L → V in NBIA1. 1 Publication
VAR_015158
Natural varianti286 – 2861R → C in NBIA1. 1 Publication
VAR_015159
Natural varianti322 – 3221E → D in NBIA1; atypical. 1 Publication
VAR_060937
Natural varianti322 – 3221E → G in NBIA1. 1 Publication
VAR_060938
Natural varianti327 – 3271T → I in NBIA1. 1 Publication
VAR_015160
Natural varianti351 – 3511S → P in NBIA1; atypical. 1 Publication
VAR_015161
Natural varianti355 – 3551N → S in NBIA1; atypical. 1 Publication
VAR_015162
Natural varianti357 – 3571R → Q in NBIA1. 1 Publication
VAR_060939
Natural varianti398 – 3981A → T in NBIA1. 1 Publication
VAR_060940
Natural varianti404 – 4041N → I in NBIA1; atypical. 1 Publication
VAR_015163
Natural varianti413 – 4131L → P in NBIA1. 1 Publication
VAR_015164
Natural varianti425 – 4251Missing in NBIA1. 1 Publication
VAR_060941
Natural varianti428 – 4281C → Y in NBIA1. 1 Publication
VAR_060942
Natural varianti447 – 4471D → N in NBIA1. 1 Publication
VAR_060943
Natural varianti471 – 4711S → N in NBIA1. 1 Publication
VAR_015165
Natural varianti497 – 4971I → T in NBIA1. 1 Publication
VAR_015166
Natural varianti500 – 5001N → I in NBIA1. 1 Publication
VAR_015167
Natural varianti501 – 5011I → T in NBIA1; atypical. 1 Publication
VAR_060944
Natural varianti509 – 5091A → V in NBIA1. 1 Publication
VAR_060945
Natural varianti511 – 5111N → D in NBIA1. 1 Publication
VAR_060946
Natural varianti521 – 5211G → R in NBIA1; classic and atypical forms. 2 Publications
VAR_015168
Natural varianti528 – 5281T → M in NBIA1; classic and atypical forms. 1 Publication
VAR_015169
Natural varianti532 – 5321R → W in NBIA1. 1 Publication
VAR_060947
Natural varianti563 – 5631L → P in NBIA1. 1 Publication
VAR_060948
Natural varianti570 – 5701P → L in NBIA1; atypical. 2 Publications
Corresponds to variant rs41279408 [ dbSNP | Ensembl ].
VAR_060949
Hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa, and pallidal degeneration (HARP)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare syndrome with many clinical similarities to PKAN.

See also OMIM:607236

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi234200. phenotype.
607236. phenotype.
Orphaneti216873. Atypical pantothenate kinase-associated neurodegeneration.
216866. Classic pantothenate kinase-associated neurodegeneration.
PharmGKBiPA38048.

Polymorphism and mutation databases

BioMutaiPANK2.
DMDMi118572682.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
BLAST
Chaini47 – 570524Pantothenate kinase 2, mitochondrialPRO_0000023201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681Phosphoserine4 Publications
Modified residuei169 – 1691Phosphoserine2 Publications
Modified residuei189 – 1891Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BZ23.
PaxDbiQ9BZ23.
PRIDEiQ9BZ23.

PTM databases

PhosphoSiteiQ9BZ23.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9BZ23.
CleanExiHS_PANK2.
ExpressionAtlasiQ9BZ23. baseline and differential.
GenevisibleiQ9BZ23. HS.

Organism-specific databases

HPAiHPA008440.
HPA021795.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX36Q9H2U11EBI-1058434,EBI-1047643
LXNQ9BS401EBI-1058434,EBI-1044504
QRICH2Q9H0J41EBI-1058434,EBI-1053637
RASGRF2O148271EBI-1058434,EBI-1055500
VDAC1P217961EBI-1058434,EBI-354158
YWHAQP273481EBI-1058434,EBI-359854

Protein-protein interaction databases

BioGridi123079. 6 interactions.
IntActiQ9BZ23. 1 interaction.
MINTiMINT-3319143.
STRINGi9606.ENSP00000313377.

Structurei

3D structure databases

ProteinModelPortaliQ9BZ23.
SMRiQ9BZ23. Positions 208-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi236 – 2438Poly-Glu

Sequence similaritiesi

Belongs to the type II pantothenate kinase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG5146.
GeneTreeiENSGT00390000020719.
HOVERGENiHBG053495.
InParanoidiQ9BZ23.
KOiK09680.
OMAiLPARWRN.
OrthoDBiEOG7R2BJR.
PhylomeDBiQ9BZ23.
TreeFamiTF314866.

Family and domain databases

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

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q9BZ23-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRLGPFHPR VHWAAPPSLS SGLHRLLFLR GTRIPSSTTL SPPRHDSLSL
60 70 80 90 100
DGGTVNPPRV REPTGREAFG PSPASSDWLP ARWRNGRGGR PRARLCSGWT
110 120 130 140 150
AAEEARRNPT LGGLLGRQRL LLRMGGGRLG APMERHGRAS ATSVSSAGEQ
160 170 180 190 200
AAGDPEGRRQ EPLRRRASSA SVPAVGASAE GTRRDRLGSY SGPTSVSRQR
210 220 230 240 250
VESLRKKRPL FPWFGLDIGG TLVKLVYFEP KDITAEEEEE EVESLKSIRK
260 270 280 290 300
YLTSNVAYGS TGIRDVHLEL KDLTLCGRKG NLHFIRFPTH DMPAFIQMGR
310 320 330 340 350
DKNFSSLHTV FCATGGGAYK FEQDFLTIGD LQLCKLDELD CLIKGILYID
360 370 380 390 400
SVGFNGRSQC YYFENPADSE KCQKLPFDLK NPYPLLLVNI GSGVSILAVY
410 420 430 440 450
SKDNYKRVTG TSLGGGTFFG LCCLLTGCTT FEEALEMASR GDSTKVDKLV
460 470 480 490 500
RDIYGGDYER FGLPGWAVAS SFGNMMSKEK REAVSKEDLA RATLITITNN
510 520 530 540 550
IGSIARMCAL NENINQVVFV GNFLRINTIA MRLLAYALDY WSKGQLKALF
560 570
SEHEGYFGAV GALLELLKIP
Length:570
Mass (Da):62,681
Last modified:November 28, 2006 - v3
Checksum:i9061A60D6CA93BBB
GO
Isoform 3 (identifier: Q9BZ23-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-291: Missing.

Show »
Length:279
Mass (Da):30,753
Checksum:iF5702EFD761FEB2B
GO
Isoform 2 (identifier: Q9BZ23-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Note: Produced by alternative initiation at Met-124 of isoform 1.
Show »
Length:447
Mass (Da):49,117
Checksum:i07B4333A838BD6A8
GO
Isoform 4 (identifier: Q9BZ23-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
     111-111: L → M

Note: May be produced by alternative initiation at Leu-111 of isoform 1. No experimental confirmation available.
Show »
Length:460
Mass (Da):50,582
Checksum:i5453A42C35481D52
GO

Sequence cautioni

The sequence BAC05173.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti460 – 4601R → G in BAB13897 (PubMed:14702039).Curated
Sequence conflicti475 – 4751M → K in BAB13897 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941R → P.1 Publication
Corresponds to variant rs71647827 [ dbSNP | Ensembl ].
VAR_054484
Natural varianti111 – 1111L → Q.2 Publications
Corresponds to variant rs71647828 [ dbSNP | Ensembl ].
VAR_015152
Natural varianti126 – 1261G → A.3 Publications
Corresponds to variant rs3737084 [ dbSNP | Ensembl ].
VAR_015153
Natural varianti134 – 1341E → G in NBIA1. 1 Publication
VAR_060934
Natural varianti219 – 2191G → V in NBIA1; atypical. 1 Publication
VAR_015154
Natural varianti234 – 2341T → A in NBIA1; atypical. 1 Publication
VAR_015155
Natural varianti249 – 2491R → P in NBIA1. 1 Publication
VAR_060935
Natural varianti264 – 2641R → W in NBIA1. 1 Publication
VAR_015156
Natural varianti278 – 2781R → C in NBIA1; atypical. 1 Publication
VAR_015157
Natural varianti278 – 2781R → L in NBIA1. 1 Publication
VAR_060936
Natural varianti282 – 2821L → V in NBIA1. 1 Publication
VAR_015158
Natural varianti286 – 2861R → C in NBIA1. 1 Publication
VAR_015159
Natural varianti322 – 3221E → D in NBIA1; atypical. 1 Publication
VAR_060937
Natural varianti322 – 3221E → G in NBIA1. 1 Publication
VAR_060938
Natural varianti327 – 3271T → I in NBIA1. 1 Publication
VAR_015160
Natural varianti351 – 3511S → P in NBIA1; atypical. 1 Publication
VAR_015161
Natural varianti355 – 3551N → S in NBIA1; atypical. 1 Publication
VAR_015162
Natural varianti357 – 3571R → Q in NBIA1. 1 Publication
VAR_060939
Natural varianti398 – 3981A → T in NBIA1. 1 Publication
VAR_060940
Natural varianti404 – 4041N → I in NBIA1; atypical. 1 Publication
VAR_015163
Natural varianti413 – 4131L → P in NBIA1. 1 Publication
VAR_015164
Natural varianti425 – 4251Missing in NBIA1. 1 Publication
VAR_060941
Natural varianti428 – 4281C → Y in NBIA1. 1 Publication
VAR_060942
Natural varianti447 – 4471D → N in NBIA1. 1 Publication
VAR_060943
Natural varianti471 – 4711S → N in NBIA1. 1 Publication
VAR_015165
Natural varianti497 – 4971I → T in NBIA1. 1 Publication
VAR_015166
Natural varianti500 – 5001N → I in NBIA1. 1 Publication
VAR_015167
Natural varianti501 – 5011I → T in NBIA1; atypical. 1 Publication
VAR_060944
Natural varianti509 – 5091A → V in NBIA1. 1 Publication
VAR_060945
Natural varianti511 – 5111N → D in NBIA1. 1 Publication
VAR_060946
Natural varianti521 – 5211G → R in NBIA1; classic and atypical forms. 2 Publications
VAR_015168
Natural varianti528 – 5281T → M in NBIA1; classic and atypical forms. 1 Publication
VAR_015169
Natural varianti532 – 5321R → W in NBIA1. 1 Publication
VAR_060947
Natural varianti563 – 5631L → P in NBIA1. 1 Publication
VAR_060948
Natural varianti570 – 5701P → L in NBIA1; atypical. 2 Publications
Corresponds to variant rs41279408 [ dbSNP | Ensembl ].
VAR_060949

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 291291Missing in isoform 3. 1 PublicationVSP_007424Add
BLAST
Alternative sequencei1 – 123123Missing in isoform 2. CuratedVSP_018825Add
BLAST
Alternative sequencei1 – 110110Missing in isoform 4. CuratedVSP_038494Add
BLAST
Alternative sequencei111 – 1111L → M in isoform 4. CuratedVSP_038495

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF494409 mRNA. Translation: AAN32907.1.
AK021791 mRNA. Translation: BAB13897.1.
AK097796 mRNA. Translation: BAC05173.1. Different initiation.
EU595875 Genomic DNA. Translation: ACD11492.1.
AL353194, AL031670 Genomic DNA. Translation: CAI11036.1.
AL353194, AL031670 Genomic DNA. Translation: CAI11037.1.
AL031670, AL353194 Genomic DNA. Translation: CAI22385.1.
AL031670, AL353194 Genomic DNA. Translation: CAI22386.1.
CH471133 Genomic DNA. Translation: EAX10478.1.
CH471133 Genomic DNA. Translation: EAX10476.1.
AL713654 mRNA. Translation: CAD28463.1.
BK000010 mRNA. Translation: DAA00004.1.
CCDSiCCDS13071.2. [Q9BZ23-1]
CCDS13072.1. [Q9BZ23-2]
RefSeqiNP_079236.3. NM_024960.4. [Q9BZ23-2]
NP_705902.2. NM_153638.2. [Q9BZ23-1]
NP_705904.1. NM_153640.2. [Q9BZ23-2]
XP_005260893.3. XM_005260836.3. [Q9BZ23-2]
XP_006723694.1. XM_006723631.1. [Q9BZ23-2]
UniGeneiHs.516859.

Genome annotation databases

EnsembliENST00000316562; ENSP00000313377; ENSG00000125779.
ENST00000497424; ENSP00000417609; ENSG00000125779. [Q9BZ23-2]
ENST00000610179; ENSP00000477429; ENSG00000125779. [Q9BZ23-3]
ENST00000621507; ENSP00000481523; ENSG00000125779. [Q9BZ23-2]
GeneIDi80025.
KEGGihsa:80025.
UCSCiuc002wkb.3. human. [Q9BZ23-2]
uc002wkc.3. human. [Q9BZ23-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF494409 mRNA. Translation: AAN32907.1.
AK021791 mRNA. Translation: BAB13897.1.
AK097796 mRNA. Translation: BAC05173.1. Different initiation.
EU595875 Genomic DNA. Translation: ACD11492.1.
AL353194, AL031670 Genomic DNA. Translation: CAI11036.1.
AL353194, AL031670 Genomic DNA. Translation: CAI11037.1.
AL031670, AL353194 Genomic DNA. Translation: CAI22385.1.
AL031670, AL353194 Genomic DNA. Translation: CAI22386.1.
CH471133 Genomic DNA. Translation: EAX10478.1.
CH471133 Genomic DNA. Translation: EAX10476.1.
AL713654 mRNA. Translation: CAD28463.1.
BK000010 mRNA. Translation: DAA00004.1.
CCDSiCCDS13071.2. [Q9BZ23-1]
CCDS13072.1. [Q9BZ23-2]
RefSeqiNP_079236.3. NM_024960.4. [Q9BZ23-2]
NP_705902.2. NM_153638.2. [Q9BZ23-1]
NP_705904.1. NM_153640.2. [Q9BZ23-2]
XP_005260893.3. XM_005260836.3. [Q9BZ23-2]
XP_006723694.1. XM_006723631.1. [Q9BZ23-2]
UniGeneiHs.516859.

3D structure databases

ProteinModelPortaliQ9BZ23.
SMRiQ9BZ23. Positions 208-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123079. 6 interactions.
IntActiQ9BZ23. 1 interaction.
MINTiMINT-3319143.
STRINGi9606.ENSP00000313377.

PTM databases

PhosphoSiteiQ9BZ23.

Polymorphism and mutation databases

BioMutaiPANK2.
DMDMi118572682.

Proteomic databases

MaxQBiQ9BZ23.
PaxDbiQ9BZ23.
PRIDEiQ9BZ23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316562; ENSP00000313377; ENSG00000125779.
ENST00000497424; ENSP00000417609; ENSG00000125779. [Q9BZ23-2]
ENST00000610179; ENSP00000477429; ENSG00000125779. [Q9BZ23-3]
ENST00000621507; ENSP00000481523; ENSG00000125779. [Q9BZ23-2]
GeneIDi80025.
KEGGihsa:80025.
UCSCiuc002wkb.3. human. [Q9BZ23-2]
uc002wkc.3. human. [Q9BZ23-1]

Organism-specific databases

CTDi80025.
GeneCardsiGC20P003869.
GeneReviewsiPANK2.
HGNCiHGNC:15894. PANK2.
HPAiHPA008440.
HPA021795.
MIMi234200. phenotype.
606157. gene.
607236. phenotype.
neXtProtiNX_Q9BZ23.
Orphaneti216873. Atypical pantothenate kinase-associated neurodegeneration.
216866. Classic pantothenate kinase-associated neurodegeneration.
PharmGKBiPA38048.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5146.
GeneTreeiENSGT00390000020719.
HOVERGENiHBG053495.
InParanoidiQ9BZ23.
KOiK09680.
OMAiLPARWRN.
OrthoDBiEOG7R2BJR.
PhylomeDBiQ9BZ23.
TreeFamiTF314866.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00352.
BRENDAi2.7.1.33. 2681.
ReactomeiREACT_11218. Coenzyme A biosynthesis.
SABIO-RKQ9BZ23.

Miscellaneous databases

ChiTaRSiPANK2. human.
GeneWikiiPANK2_(gene).
GenomeRNAii80025.
NextBioi70178.
PROiQ9BZ23.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZ23.
CleanExiHS_PANK2.
ExpressionAtlasiQ9BZ23. baseline and differential.
GenevisibleiQ9BZ23. HS.

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. "An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria."
    Hoertnagel K., Prokisch H., Meitinger T.
    Hum. Mol. Genet. 12:321-327(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-126, SUBCELLULAR LOCATION.
    Tissue: Brain.
  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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-570 (ISOFORM 1).
    Tissue: Testis.
  3. NIEHS SNPs program
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-94; GLN-111 AND ALA-126.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-570.
    Tissue: Brain.
  7. "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: IDENTIFICATION, ALTERNATIVE INITIATION AT LEU-111, VARIANTS GLN-111 AND ALA-126, VARIANTS NBIA1 VAL-219; ALA-234; TRP-264; CYS-278; VAL-282; CYS-286; ILE-327; PRO-351; SER-355; ILE-404; PRO-413; ASN-471; THR-497; ILE-500; ARG-521 AND MET-528, TISSUE SPECIFICITY.
  8. "HARP syndrome is allelic with pantothenate kinase-associated neurodegeneration."
    Ching K.H.L., Westaway S.K., Gitschier J., Higgins J.J., Hayflick S.J.
    Neurology 58:1673-1674(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HARP.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-169 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-169 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome."
    Hayflick S.J., Westaway S.K., Levinson B., Zhou B., Johnson M.A., Ching K.H., Gitschier J.
    N. Engl. J. Med. 348:33-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NBIA1 GLY-134; PRO-249; LEU-278; ASP-322; GLY-322; GLN-357; THR-398; LEU-425 DEL; TYR-428; ASN-447; THR-501; VAL-509; ASP-511; TRP-532; PRO-563 AND LEU-570.
  16. "Atypical Hallervorden-Spatz disease with preserved cognition and obtrusive obsessions and compulsions."
    Nicholas A.P., Earnst K.S., Marson D.C.
    Mov. Disord. 20:880-886(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NBIA1 ARG-521 AND LEU-570.

Entry informationi

Entry nameiPANK2_HUMAN
AccessioniPrimary (citable) accession number: Q9BZ23
Secondary accession number(s): B1AK33
, B2Z3X0, D3DVZ0, Q5T7I2, Q5T7I4, Q7RTX5, Q8N7Q4, Q8TCR5, Q9BYW5, Q9HAF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 28, 2006
Last modified: July 22, 2015
This is version 137 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

Miscellaneous

The HSS syndrome has been proposed to be renamed because of the unethical activities of Julius Hallervorden and Hugo Spatz during world war II.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.