PANK2_HUMAN - dbPTM
PANK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PANK2_HUMAN
UniProt AC Q9BZ23
Protein Name Pantothenate kinase 2, mitochondrial
Gene Name PANK2
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Isoform 1: Mitochondrion.
Isoform 2: Cytoplasm .
Isoform 3: Cytoplasm .
Isoform 4: Cytoplasm .
Protein Description May be the master regulator of the CoA biosynthesis..
Protein Sequence MRRLGPFHPRVHWAAPPSLSSGLHRLLFLRGTRIPSSTTLSPPRHDSLSLDGGTVNPPRVREPTGREAFGPSPASSDWLPARWRNGRGGRPRARLCSGWTAAEEARRNPTLGGLLGRQRLLLRMGGGRLGAPMERHGRASATSVSSAGEQAAGDPEGRRQEPLRRRASSASVPAVGASAEGTRRDRLGSYSGPTSVSRQRVESLRKKRPLFPWFGLDIGGTLVKLVYFEPKDITAEEEEEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDMPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDSVGFNGRSQCYYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAMRLLAYALDYWSKGQLKALFSEHEGYFGAVGALLELLKIP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
41PhosphorylationIPSSTTLSPPRHDSL
CCCCCCCCCCCCCCC		30.6624719451
123 (in isoform 3)Ubiquitination-22.9721890473
127 (in isoform 3)Ubiquitination-18.8621890473
140 (in isoform 4)Ubiquitination-30.6221890473
140PhosphorylationMERHGRASATSVSSA
HHHHCCCCCCCCCHH		30.6226657352
142PhosphorylationRHGRASATSVSSAGE
HHCCCCCCCCCHHHH		27.4529978859
143PhosphorylationHGRASATSVSSAGEQ
HCCCCCCCCCHHHHH		21.5129978859
145PhosphorylationRASATSVSSAGEQAA
CCCCCCCCHHHHHHC		17.7829978859
146PhosphorylationASATSVSSAGEQAAG
CCCCCCCHHHHHHCC		37.8321815630
168PhosphorylationEPLRRRASSASVPAV
HHHHHHHHCCCCCCC		25.3229255136
169PhosphorylationPLRRRASSASVPAVG
HHHHHHHCCCCCCCC		24.4729255136
171PhosphorylationRRRASSASVPAVGAS
HHHHHCCCCCCCCCC		30.4922167270
178PhosphorylationSVPAVGASAEGTRRD
CCCCCCCCCCCCCCC		22.4123927012
182O-linked_GlycosylationVGASAEGTRRDRLGS
CCCCCCCCCCCCCCC		17.6530379171
182PhosphorylationVGASAEGTRRDRLGS
CCCCCCCCCCCCCCC		17.6523927012
189PhosphorylationTRRDRLGSYSGPTSV
CCCCCCCCCCCCCHH		22.2519664994
190PhosphorylationRRDRLGSYSGPTSVS
CCCCCCCCCCCCHHH		18.8227273156
191PhosphorylationRDRLGSYSGPTSVSR
CCCCCCCCCCCHHHH		39.7429255136
194PhosphorylationLGSYSGPTSVSRQRV
CCCCCCCCHHHHHHH		45.3323927012
195PhosphorylationGSYSGPTSVSRQRVE
CCCCCCCHHHHHHHH		22.6423927012
197PhosphorylationYSGPTSVSRQRVESL
CCCCCHHHHHHHHHH		23.5923403867
203PhosphorylationVSRQRVESLRKKRPL
HHHHHHHHHHHHCCC		30.5325106551
227PhosphorylationGTLVKLVYFEPKDIT
CEEEEEEEECCCCCC		16.8029496907
231UbiquitinationKLVYFEPKDITAEEE
EEEEECCCCCCCCHH		55.34-
246 (in isoform 1)Ubiquitination-53.7921890473
246UbiquitinationEEEVESLKSIRKYLT
HHHHHHHHHHHHHHH		53.792190698
250MalonylationESLKSIRKYLTSNVA
HHHHHHHHHHHCCCC		42.8326320211
250UbiquitinationESLKSIRKYLTSNVA
HHHHHHHHHHHCCCC		42.83-
250 (in isoform 1)Ubiquitination-42.8321890473
252UbiquitinationLKSIRKYLTSNVAYG
HHHHHHHHHCCCCCC		4.8021890473
252 (in isoform 2)Ubiquitination-4.8021890473
271UbiquitinationRDVHLELKDLTLCGR
CEEEEEEEECEECCC		41.12-
279UbiquitinationDLTLCGRKGNLHFIR
ECEECCCCCCEEEEE		37.12-
371UbiquitinationENPADSEKCQKLPFD
CCCCCHHHHCCCCCC		46.01-
395PhosphorylationVNIGSGVSILAVYSK
EEECCCEEEEEEEEC		18.53-
400PhosphorylationGVSILAVYSKDNYKR
CEEEEEEEECCCCEE		12.37-
405PhosphorylationAVYSKDNYKRVTGTS
EEEECCCCEECEEEE		15.42-
420 (in isoform 3)Ubiquitination-17.3921890473
433 (in isoform 4)Ubiquitination-55.1321890473
458PhosphorylationRDIYGGDYERFGLPG
HHHHCCCHHHHCCCH		16.5727642862
470PhosphorylationLPGWAVASSFGNMMS
CCHHHHHHHHHHHCC		21.43-
471PhosphorylationPGWAVASSFGNMMSK
CHHHHHHHHHHHCCH		27.69-
477PhosphorylationSSFGNMMSKEKREAV
HHHHHHCCHHHHHHC		27.22-
478UbiquitinationSFGNMMSKEKREAVS
HHHHHCCHHHHHHCC		49.73-
480UbiquitinationGNMMSKEKREAVSKE
HHHCCHHHHHHCCHH		60.31-
486UbiquitinationEKREAVSKEDLARAT
HHHHHCCHHHHHHHH		48.96-
543 (in isoform 1)Ubiquitination-36.2121890473
543UbiquitinationYALDYWSKGQLKALF
HHHHHCCHHHHHHHH		36.21-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PANK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PANK2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PANK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LXN_HUMANLXNphysical
17353931
VDAC1_HUMANVDAC1physical
17353931
DHX36_HUMANDHX36physical
17353931
RGRF2_HUMANRASGRF2physical
17353931
QRIC2_HUMANQRICH2physical
17353931
UBB_HUMANUBBphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
NECT2_HUMANPVRL2physical
28514442
KI13B_HUMANKIF13Bphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CING_HUMANCGNphysical
27173435
CBY1_HUMANCBY1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
234200Neurodegeneration with brain iron accumulation 1 (NBIA1)
607236Hypoprebetalipoproteinemia, acanthocytosis, retinitis pigmentosa, and pallidal degeneration (HARP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PANK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-169 ANDSER-189, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-169 ANDSER-189, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168; SER-169 ANDSER-189, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.

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