UAP1_HUMAN - dbPTM
UAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UAP1_HUMAN
UniProt AC Q16222
Protein Name UDP-N-acetylhexosamine pyrophosphorylase
Gene Name UAP1
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cytoplasm. In spermatozoa, localized to the principal piece of the tail, the neck region of the head and to a lesser extent, the midpiece of the tail.
Protein Description Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P..
Protein Sequence MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
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
7Ubiquitination-MNINDLKLTLSKAG
-CCHHHHHHHHHHHH		42.14-
12UbiquitinationDLKLTLSKAGQEHLL
HHHHHHHHHHHHHHH		60.7021890473
12 (in isoform 1)Ubiquitination-60.7021890473
12 (in isoform 2)Ubiquitination-60.7021890473
12 (in isoform 3)Ubiquitination-60.7021890473
59PhosphorylationAIEGFNQSSHQKNVD
HHHCCCCCHHCCCCC		30.7830576142
63 (in isoform 2)Ubiquitination-54.2221890473
63AcetylationFNQSSHQKNVDARME
CCCCHHCCCCCHHCC		54.2226210075
63 (in isoform 1)Ubiquitination-54.2221890473
63 (in isoform 3)Ubiquitination-54.2221890473
63UbiquitinationFNQSSHQKNVDARME
CCCCHHCCCCCHHCC		54.2221890473
81PhosphorylationREVLGSATRDQDQLQ
HHHHCCCCCCHHHHH		36.1530576142
122UbiquitinationRLGVAYPKGMYDVGL
EEEEEECCCCCCCCC		43.57-
125PhosphorylationVAYPKGMYDVGLPSR
EEECCCCCCCCCCCC		19.0220090780
133UbiquitinationDVGLPSRKTLFQIQA
CCCCCCCCHHHHHHH		54.65-
145UbiquitinationIQAERILKLQQVAEK
HHHHHHHHHHHHHHH		41.71-
152UbiquitinationKLQQVAEKYYGNKCI
HHHHHHHHHHCCCCE		33.75-
152AcetylationKLQQVAEKYYGNKCI
HHHHHHHHHHCCCCE		33.7526051181
153PhosphorylationLQQVAEKYYGNKCII
HHHHHHHHHCCCCEE		14.22-
157UbiquitinationAEKYYGNKCIIPWYI
HHHHHCCCCEEEEEE		23.58-
170PhosphorylationYIMTSGRTMESTKEF
EEECCCCCHHHHHHH		28.90-
175UbiquitinationGRTMESTKEFFTKHK
CCCHHHHHHHHHHCC		62.90-
175AcetylationGRTMESTKEFFTKHK
CCCHHHHHHHHHHCC		62.9027452117
180UbiquitinationSTKEFFTKHKYFGLK
HHHHHHHHCCCCCCC		32.7019608861
180AcetylationSTKEFFTKHKYFGLK
HHHHHHHHCCCCCCC		32.7019608861
182AcetylationKEFFTKHKYFGLKKE
HHHHHHCCCCCCCHH		43.7825953088
182UbiquitinationKEFFTKHKYFGLKKE
HHHHHHCCCCCCCHH		43.78-
182MalonylationKEFFTKHKYFGLKKE
HHHHHHCCCCCCCHH		43.7826320211
188UbiquitinationHKYFGLKKENVIFFQ
CCCCCCCHHCEEEEE		60.61-
213UbiquitinationGKIILEEKNKVSMAP
CEEEEEECCCEEECC		53.33-
215UbiquitinationIILEEKNKVSMAPDG
EEEEECCCEEECCCC		46.91-
239SulfoxidationAQNIVEDMEQRGIWS
HCCHHHHHHHCCCCE		2.7521406390
271AcetylationFIGFCIQKGADCGAK
CEEEEECCCCCCCCE		35.8326051181
271UbiquitinationFIGFCIQKGADCGAK
CEEEEECCCCCCCCE		35.83-
278UbiquitinationKGADCGAKVVEKTNP
CCCCCCCEEEECCCC		31.90-
278AcetylationKGADCGAKVVEKTNP
CCCCCCCEEEECCCC		31.9027452117
282UbiquitinationCGAKVVEKTNPTEPV
CCCEEEECCCCCCCC		41.83-
293S-nitrosylationTEPVGVVCRVDGVYQ
CCCCEEEEEECCEEE		3.052212679
299PhosphorylationVCRVDGVYQVVEYSE
EEEECCEEEEEEEEE		10.91-
304PhosphorylationGVYQVVEYSEISLAT
CEEEEEEEEEEEEEE		10.45-
314UbiquitinationISLATAQKRSSDGRL
EEEEECHHCCCCCCE		52.35-
356MalonylationLQHHVAQKKIPYVDT
HHHHHHCCCCCCCCC		42.8226320211
356UbiquitinationLQHHVAQKKIPYVDT
HHHHHHCCCCCCCCC		42.82-
357UbiquitinationQHHVAQKKIPYVDTQ
HHHHHCCCCCCCCCC		36.51-
360PhosphorylationVAQKKIPYVDTQGQL
HHCCCCCCCCCCCCE		17.90-
363PhosphorylationKKIPYVDTQGQLIKP
CCCCCCCCCCCEECC		25.26-
369UbiquitinationDTQGQLIKPDKPNGI
CCCCCEECCCCCCCC		56.61-
372UbiquitinationGQLIKPDKPNGIKME
CCEECCCCCCCCEEH		49.24-
372AcetylationGQLIKPDKPNGIKME
CCEECCCCCCCCEEH		49.2426051181
377UbiquitinationPDKPNGIKMEKFVFD
CCCCCCCEEHHHHHH		42.26-
380UbiquitinationPNGIKMEKFVFDIFQ
CCCCEEHHHHHHHHH		43.24-
390 (in isoform 3)Ubiquitination-48.2921890473
390 (in isoform 2)Ubiquitination-48.2921890473
390UbiquitinationFDIFQFAKKFVVYEV
HHHHHHHHHHHHHHH		48.2921906983
390 (in isoform 1)Ubiquitination-48.2921890473
391UbiquitinationDIFQFAKKFVVYEVL
HHHHHHHHHHHHHHH		39.71-
395PhosphorylationFAKKFVVYEVLREDE
HHHHHHHHHHHCCCC		8.6023898821
404PhosphorylationVLREDEFSPLKNADS
HHCCCCCCCCCCCCC		27.5521815630
407UbiquitinationEDEFSPLKNADSQNG
CCCCCCCCCCCCCCC		54.17-
415 (in isoform 1)Ubiquitination-62.9821890473
415UbiquitinationNADSQNGKDNPTTAR
CCCCCCCCCCHHHHH		62.982190698
415 (in isoform 2)Ubiquitination-62.9821890473
415 (in isoform 3)Ubiquitination-62.9821890473
459AcetylationPRSATNGKSETITAD
CCCCCCCCCCEEEEE		47.3823236377
472AcetylationADVNHNLKDANDVPI
EECCCCCCCCCCCEE		61.187704293
502UbiquitinationESYVADKEFHAPLII
HHHHCCCCCCCCEEE		43.12-
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 UAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UAP1_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 UAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UAP1_HUMANUAP1physical
11707391
VASP_HUMANVASPphysical
22939629
VPS39_HUMANVPS39physical
22939629
UAP1_HUMANUAP1physical
25416956
PABP1_HUMANPABPC1physical
26344197
AGM1_HUMANPGM3physical
26344197
SCLY_HUMANSCLYphysical
26344197
SDHB_HUMANSDHBphysical
26344197
WDR1_HUMANWDR1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UAP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS SPECTROMETRY.

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