Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BZ23 (PANK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate kinase 2, mitochondrial

Short name=hPanK2
EC=2.7.1.33
Alternative name(s):
Pantothenic acid kinase 2
Gene names
Name:PANK2
Synonyms:C20orf48
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Regulated by feedback inhibition by CoA and its thioesters.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Isoform 1: Mitochondrion Ref.1.

Isoform 2: Cytoplasm Potential Ref.1.

Isoform 3: Cytoplasm Potential Ref.1.

Isoform 4: Cytoplasm Potential Ref.1.

Tissue specificity

Ubiquitous. Ref.7

Involvement in disease

Neurodegeneration with brain iron accumulation 1 (NBIA1) [MIM:234200]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.14 Ref.15

Hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa, and pallidal degeneration (HARP) [MIM:607236]: Rare syndrome with many clinical similarities to PKAN.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

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.

Sequence similarities

Belongs to the type II pantothenate kinase family.

Sequence caution

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

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic respiration

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

coenzyme A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

coenzyme biosynthetic process

Traceable author statement. Source: Reactome

mitochondrion morphogenesis

Inferred from electronic annotation. Source: Ensembl

pantothenate metabolic process

Traceable author statement. Source: Reactome

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

spermatid development

Inferred from electronic annotation. Source: Ensembl

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantothenate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q9BZ23-1)

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.
Isoform 3 (identifier: Q9BZ23-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-291: Missing.
Isoform 2 (identifier: Q9BZ23-3)

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.
Isoform 4 (identifier: Q9BZ23-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 570524Pantothenate kinase 2, mitochondrial
PRO_0000023201

Regions

Compositional bias236 – 2438Poly-Glu

Sites

Binding site3921Acetyl-CoA By similarity
Binding site3951Acetyl-CoA By similarity
Binding site4071Acetyl-CoA By similarity

Amino acid modifications

Modified residue1681Phosphoserine Ref.10 Ref.11 Ref.13
Modified residue1691Phosphoserine Ref.10 Ref.11
Modified residue1891Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13

Natural variations

Alternative sequence1 – 291291Missing in isoform 3.
VSP_007424
Alternative sequence1 – 123123Missing in isoform 2.
VSP_018825
Alternative sequence1 – 110110Missing in isoform 4.
VSP_038494
Alternative sequence1111L → M in isoform 4.
VSP_038495
Natural variant941R → P. Ref.3
Corresponds to variant rs71647827 [ dbSNP | Ensembl ].
VAR_054484
Natural variant1111L → Q. Ref.3 Ref.7
Corresponds to variant rs71647828 [ dbSNP | Ensembl ].
VAR_015152
Natural variant1261G → A. Ref.1 Ref.3 Ref.7
Corresponds to variant rs3737084 [ dbSNP | Ensembl ].
VAR_015153
Natural variant1341E → G in NBIA1. Ref.14
VAR_060934
Natural variant2191G → V in NBIA1; atypical. Ref.7
VAR_015154
Natural variant2341T → A in NBIA1; atypical. Ref.7
VAR_015155
Natural variant2491R → P in NBIA1. Ref.14
VAR_060935
Natural variant2641R → W in NBIA1. Ref.7
VAR_015156
Natural variant2781R → C in NBIA1; atypical. Ref.7
VAR_015157
Natural variant2781R → L in NBIA1. Ref.14
VAR_060936
Natural variant2821L → V in NBIA1. Ref.7
VAR_015158
Natural variant2861R → C in NBIA1. Ref.7
VAR_015159
Natural variant3221E → D in NBIA1; atypical. Ref.14
VAR_060937
Natural variant3221E → G in NBIA1. Ref.14
VAR_060938
Natural variant3271T → I in NBIA1. Ref.7
VAR_015160
Natural variant3511S → P in NBIA1; atypical. Ref.7
VAR_015161
Natural variant3551N → S in NBIA1; atypical. Ref.7
VAR_015162
Natural variant3571R → Q in NBIA1. Ref.14
VAR_060939
Natural variant3981A → T in NBIA1. Ref.14
VAR_060940
Natural variant4041N → I in NBIA1; atypical. Ref.7
VAR_015163
Natural variant4131L → P in NBIA1. Ref.7
VAR_015164
Natural variant4251Missing in NBIA1. Ref.14
VAR_060941
Natural variant4281C → Y in NBIA1. Ref.14
VAR_060942
Natural variant4471D → N in NBIA1. Ref.14
VAR_060943
Natural variant4711S → N in NBIA1. Ref.7
VAR_015165
Natural variant4971I → T in NBIA1. Ref.7
VAR_015166
Natural variant5001N → I in NBIA1. Ref.7
VAR_015167
Natural variant5011I → T in NBIA1; atypical. Ref.14
VAR_060944
Natural variant5091A → V in NBIA1. Ref.14
VAR_060945
Natural variant5111N → D in NBIA1. Ref.14
VAR_060946
Natural variant5211G → R in NBIA1; classic and atypical forms. Ref.7 Ref.15
VAR_015168
Natural variant5281T → M in NBIA1; classic and atypical forms. Ref.7
VAR_015169
Natural variant5321R → W in NBIA1. Ref.14
VAR_060947
Natural variant5631L → P in NBIA1. Ref.14
VAR_060948
Natural variant5701P → L in NBIA1; atypical. Ref.14 Ref.15
Corresponds to variant rs41279408 [ dbSNP | Ensembl ].
VAR_060949

Experimental info

Sequence conflict4601R → G in BAB13897. Ref.2
Sequence conflict4751M → K in BAB13897. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: 9061A60D6CA93BBB

FASTA57062,681
        10         20         30         40         50         60 
MRRLGPFHPR VHWAAPPSLS SGLHRLLFLR GTRIPSSTTL SPPRHDSLSL DGGTVNPPRV 

        70         80         90        100        110        120 
REPTGREAFG PSPASSDWLP ARWRNGRGGR PRARLCSGWT AAEEARRNPT LGGLLGRQRL 

       130        140        150        160        170        180 
LLRMGGGRLG APMERHGRAS ATSVSSAGEQ AAGDPEGRRQ EPLRRRASSA SVPAVGASAE 

       190        200        210        220        230        240 
GTRRDRLGSY SGPTSVSRQR VESLRKKRPL FPWFGLDIGG TLVKLVYFEP KDITAEEEEE 

       250        260        270        280        290        300 
EVESLKSIRK YLTSNVAYGS TGIRDVHLEL KDLTLCGRKG NLHFIRFPTH DMPAFIQMGR 

       310        320        330        340        350        360 
DKNFSSLHTV FCATGGGAYK FEQDFLTIGD LQLCKLDELD CLIKGILYID SVGFNGRSQC 

       370        380        390        400        410        420 
YYFENPADSE KCQKLPFDLK NPYPLLLVNI GSGVSILAVY SKDNYKRVTG TSLGGGTFFG 

       430        440        450        460        470        480 
LCCLLTGCTT FEEALEMASR GDSTKVDKLV RDIYGGDYER FGLPGWAVAS SFGNMMSKEK 

       490        500        510        520        530        540 
REAVSKEDLA RATLITITNN IGSIARMCAL NENINQVVFV GNFLRINTIA MRLLAYALDY 

       550        560        570 
WSKGQLKALF SEHEGYFGAV GALLELLKIP 

« Hide

Isoform 3 [UniParc].

Checksum: F5702EFD761FEB2B
Show »

FASTA27930,753
Isoform 2 [UniParc].

Checksum: 07B4333A838BD6A8
Show »

FASTA44749,117
Isoform 4 [UniParc].

Checksum: 5453A42C35481D52
Show »

FASTA46050,582

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]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].
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [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: 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]"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.
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_079236.3. NM_024960.4.
NP_705902.2. NM_153638.2.
NP_705904.1. NM_153640.2.
UniGeneHs.516859.

3D structure databases

ProteinModelPortalQ9BZ23.
SMRQ9BZ23. Positions 208-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123079. 7 interactions.
IntActQ9BZ23. 1 interaction.
MINTMINT-3319143.

PTM databases

PhosphoSiteQ9BZ23.

Polymorphism databases

DMDM118572682.

Proteomic databases

PaxDbQ9BZ23.
PRIDEQ9BZ23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316562; ENSP00000313377; ENSG00000125779. [Q9BZ23-1]
ENST00000497424; ENSP00000417609; ENSG00000125779. [Q9BZ23-2]
ENST00000610179; ENSP00000477429; ENSG00000125779. [Q9BZ23-3]
GeneID80025.
KEGGhsa:80025.
UCSCuc002wkb.3. human. [Q9BZ23-2]
uc002wkc.3. human. [Q9BZ23-1]

Organism-specific databases

CTD80025.
GeneCardsGC20P003869.
HGNCHGNC:15894. PANK2.
HPAHPA008440.
HPA021795.
MIM234200. phenotype.
606157. gene.
607236. phenotype.
neXtProtNX_Q9BZ23.
Orphanet216873. Atypical pantothenate kinase-associated neurodegeneration.
216866. Classic pantothenate kinase-associated neurodegeneration.
PharmGKBPA38048.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5146.
HOVERGENHBG053495.
InParanoidQ9BZ23.
KOK09680.
OMANENINRV.
OrthoDBEOG7R2BJR.
PhylomeDBQ9BZ23.
TreeFamTF314866.

Enzyme and pathway databases

BRENDA2.7.1.33. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9BZ23.
UniPathwayUPA00241; UER00352.

Gene expression databases

ArrayExpressQ9BZ23.
BgeeQ9BZ23.
CleanExHS_PANK2.
GenevestigatorQ9BZ23.

Family and domain databases

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

Other

ChiTaRSPANK2. human.
GeneWikiPANK2_(gene).
GenomeRNAi80025.
NextBio70178.
PROQ9BZ23.
SOURCESearch...

Entry information

Entry namePANK2_HUMAN
AccessionPrimary (citable) accession number: Q9BZ23
Secondary accession number(s): B1AK33 expand/collapse secondary AC list , B2Z3X0, D3DVZ0, Q5T7I2, Q5T7I4, Q7RTX5, Q8N7Q4, Q8TCR5, Q9BYW5, Q9HAF2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 126 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM