OLA1_HUMAN - dbPTM
OLA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OLA1_HUMAN
UniProt AC Q9NTK5
Protein Name Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167}
Gene Name OLA1 {ECO:0000255|HAMAP-Rule:MF_03167}
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleolus . Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm.
Protein Description Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP..
Protein Sequence MPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISACDGIFHLTRAFEDDDITHVEGSVDPIRDIEIIHEELQLKDEEMIGPIIDKLEKVAVRGGDKKLKPEYDIMCKVKSWVIDQKKPVRFYHDWNDKEIEVLNKHLFLTSKPMVYLVNLSEKDYIRKKNKWLIKIKEWVDKYDPGALVIPFSGALELKLQELSAEERQKYLEANMTQSALPKIIKAGFAALQLEYFFTAGPDEVRAWTIRKGTKAPQAAGKIHTDFEKGFIMAEVMKYEDFKEEGSENAVKAAGKYRQQGRNYIVEDGDIIFFKFNTPQQPKKK
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
5Acetylation---MPPKKGGDGIKP
---CCCCCCCCCCCC		74.1125953088
11UbiquitinationKKGGDGIKPPPIIGR
CCCCCCCCCCCCCCC		57.9327667366
20UbiquitinationPPIIGRFGTSLKIGI
CCCCCCCCCCEEEEE		17.0329967540
21PhosphorylationPIIGRFGTSLKIGIV
CCCCCCCCCEEEEEE		28.33-
22PhosphorylationIIGRFGTSLKIGIVG
CCCCCCCCEEEEEEC		28.22-
30UbiquitinationLKIGIVGLPNVGKST
EEEEEECCCCCCCHH		1.6123000965
32 (in isoform 2)Ubiquitination-61.2821890473
32NeddylationIGIVGLPNVGKSTFF
EEEECCCCCCCHHHH		61.2832015554
32UbiquitinationIGIVGLPNVGKSTFF
EEEECCCCCCCHHHH		61.2823000965
39UbiquitinationNVGKSTFFNVLTNSQ
CCCCHHHHHHHCCCC		6.6529967540
51UbiquitinationNSQASAENFPFCTID
CCCHHHCCCCCEEEC		50.0029967540
55GlutathionylationSAENFPFCTIDPNES
HHCCCCCEEECCCCC		3.1222555962
58 (in isoform 2)Acetylation-23.09-
58UbiquitinationNFPFCTIDPNESRVP
CCCCEEECCCCCCCC		23.0921890473
58AcetylationNFPFCTIDPNESRVP
CCCCEEECCCCCCCC		23.0919608861
58 (in isoform 2)Ubiquitination-23.0921890473
77PhosphorylationRFDFLCQYHKPASKI
HHCHHHHCCCCHHHC		15.7128152594
79AcetylationDFLCQYHKPASKIPA
CHHHHCCCCHHHCCH		37.0325953088
79UbiquitinationDFLCQYHKPASKIPA
CHHHHCCCCHHHCCH		37.0323000965
82PhosphorylationCQYHKPASKIPAFLN
HHCCCCHHHCCHHHC		39.3828152594
83UbiquitinationQYHKPASKIPAFLNV
HCCCCHHHCCHHHCH		55.6123000965
83 (in isoform 3)Ubiquitination-55.6121890473
83 (in isoform 1)Ubiquitination-55.6121890473
84 (in isoform 2)Acetylation-2.49-
84AcetylationYHKPASKIPAFLNVV
CCCCHHHCCHHHCHH		2.4919608861
123 (in isoform 2)Ubiquitination-2.1121890473
123UbiquitinationACDGIFHLTRAFEDD
HCCCHHHHHHCCCCC		2.1123000965
136UbiquitinationDDDITHVEGSVDPIR
CCCCCEEECCCCCCH		37.8421890473
136AcetylationDDDITHVEGSVDPIR
CCCCCEEECCCCCCH		37.8419608861
136 (in isoform 2)Ubiquitination-37.8421890473
136 (in isoform 2)Acetylation-37.84-
155UbiquitinationIHEELQLKDEEMIGP
HHHHHCCCCHHHHHH		50.5732015554
1662-HydroxyisobutyrylationMIGPIIDKLEKVAVR
HHHHHHHHHHHHHCC		48.41-
166AcetylationMIGPIIDKLEKVAVR
HHHHHHHHHHHHHCC		48.4120167786
166UbiquitinationMIGPIIDKLEKVAVR
HHHHHHHHHHHHHCC		48.4133845483
168UbiquitinationGPIIDKLEKVAVRGG
HHHHHHHHHHHCCCC		51.7527667366
169UbiquitinationPIIDKLEKVAVRGGD
HHHHHHHHHHCCCCC		46.0333845483
175UbiquitinationEKVAVRGGDKKLKPE
HHHHCCCCCCCCCCC		32.7629967540
178UbiquitinationAVRGGDKKLKPEYDI
HCCCCCCCCCCCCEE		67.4929967540
180UbiquitinationRGGDKKLKPEYDIMC
CCCCCCCCCCCEEEE		44.69-
180MalonylationRGGDKKLKPEYDIMC
CCCCCCCCCCCEEEE		44.6926320211
186SulfoxidationLKPEYDIMCKVKSWV
CCCCCEEEEEEEEEE		1.3330846556
187GlutathionylationKPEYDIMCKVKSWVI
CCCCEEEEEEEEEEE		4.7222555962
188UbiquitinationPEYDIMCKVKSWVID
CCCEEEEEEEEEEEC		35.0023000965
190NeddylationYDIMCKVKSWVIDQK
CEEEEEEEEEEECCC		24.8932015554
190UbiquitinationYDIMCKVKSWVIDQK
CEEEEEEEEEEECCC		24.8923000965
190 (in isoform 3)Ubiquitination-24.8921890473
190 (in isoform 1)Ubiquitination-24.8921890473
196 (in isoform 2)Ubiquitination-44.5421890473
196UbiquitinationVKSWVIDQKKPVRFY
EEEEEECCCCCEEEE		44.5433845483
197UbiquitinationKSWVIDQKKPVRFYH
EEEEECCCCCEEEEE		56.1229967540
1972-HydroxyisobutyrylationKSWVIDQKKPVRFYH
EEEEECCCCCEEEEE		56.12-
198UbiquitinationSWVIDQKKPVRFYHD
EEEECCCCCEEEEEC		43.01-
205UbiquitinationKPVRFYHDWNDKEIE
CCEEEEECCCHHHHH		34.2029967540
205 (in isoform 2)Ubiquitination-34.2021890473
2092-HydroxyisobutyrylationFYHDWNDKEIEVLNK
EEECCCHHHHHHHHH		58.33-
209AcetylationFYHDWNDKEIEVLNK
EEECCCHHHHHHHHH		58.3323954790
209UbiquitinationFYHDWNDKEIEVLNK
EEECCCHHHHHHHHH		58.3329967540
216 (in isoform 1)Ubiquitination-37.2121890473
216 (in isoform 3)Ubiquitination-37.2121890473
216AcetylationKEIEVLNKHLFLTSK
HHHHHHHHHEEECCC		37.2119608861
216UbiquitinationKEIEVLNKHLFLTSK
HHHHHHHHHEEECCC		37.2121890473
227PhosphorylationLTSKPMVYLVNLSEK
ECCCCEEEEEECCHH		9.9321406692
232PhosphorylationMVYLVNLSEKDYIRK
EEEEEECCHHHHHHH		37.0821406692
242AcetylationDYIRKKNKWLIKIKE
HHHHHCCCEEEEHHH		52.8619608861
246AcetylationKKNKWLIKIKEWVDK
HCCCEEEEHHHHHHH		45.6227178108
248MalonylationNKWLIKIKEWVDKYD
CCEEEEHHHHHHHCC		40.2926320211
248AcetylationNKWLIKIKEWVDKYD
CCEEEEHHHHHHHCC		40.2926210075
248SumoylationNKWLIKIKEWVDKYD
CCEEEEHHHHHHHCC		40.29-
254PhosphorylationIKEWVDKYDPGALVI
HHHHHHHCCCCCEEE		23.9421406692
260UbiquitinationKYDPGALVIPFSGAL
HCCCCCEEEECCCHH		5.3223000965
264PhosphorylationGALVIPFSGALELKL
CCEEEECCCHHHHHH		20.1521406692
273UbiquitinationALELKLQELSAEERQ
HHHHHHHHCCHHHHH		55.9421890473
275PhosphorylationELKLQELSAEERQKY
HHHHHHCCHHHHHHH		32.6426699800
281UbiquitinationLSAEERQKYLEANMT
CCHHHHHHHHHHHCC		59.0123000965
281 (in isoform 1)Ubiquitination-59.0121890473
287SulfoxidationQKYLEANMTQSALPK
HHHHHHHCCHHHHHH		4.6821406390
294AcetylationMTQSALPKIIKAGFA
CCHHHHHHHHHHHHH		58.8919608861
294UbiquitinationMTQSALPKIIKAGFA
CCHHHHHHHHHHHHH		58.8921890473
294 (in isoform 1)Ubiquitination-58.8921890473
305UbiquitinationAGFAALQLEYFFTAG
HHHHHEEEEEEECCC		6.3127667366
312UbiquitinationLEYFFTAGPDEVRAW
EEEEECCCHHHHHEE		27.4329967540
323MethylationVRAWTIRKGTKAPQA
HHEEEEECCCCCCHH		68.06-
326UbiquitinationWTIRKGTKAPQAAGK
EEEECCCCCCHHCCC		67.7327667366
333UbiquitinationKAPQAAGKIHTDFEK
CCCHHCCCCCCCHHH		26.9632015554
336PhosphorylationQAAGKIHTDFEKGFI
HHCCCCCCCHHHCCE		45.95-
340AcetylationKIHTDFEKGFIMAEV
CCCCCHHHCCEEEEE		60.1425953088
340MethylationKIHTDFEKGFIMAEV
CCCCCHHHCCEEEEE		60.14115974465
3402-HydroxyisobutyrylationKIHTDFEKGFIMAEV
CCCCCHHHCCEEEEE		60.14-
342UbiquitinationHTDFEKGFIMAEVMK
CCCHHHCCEEEEEEE		5.2429967540
350PhosphorylationIMAEVMKYEDFKEEG
EEEEEEEHHHHHHHC		11.5728152594
354UbiquitinationVMKYEDFKEEGSENA
EEEHHHHHHHCCHHH		68.1521906983
354 (in isoform 1)Ubiquitination-68.1521890473
354AcetylationVMKYEDFKEEGSENA
EEEHHHHHHHCCHHH		68.1523236377
363 (in isoform 1)Ubiquitination-30.0621890473
363UbiquitinationEGSENAVKAAGKYRQ
HCCHHHHHHHHHHHH		30.062190698
363AcetylationEGSENAVKAAGKYRQ
HCCHHHHHHHHHHHH		30.0627452117
389PhosphorylationIIFFKFNTPQQPKKK
EEEEEECCCCCCCCC		26.1321815630
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 OLA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OLA1_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 OLA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
16169070
HSP74_HUMANHSPA4physical
23412384
CHIP_HUMANSTUB1physical
23412384
HMGA1_HUMANHMGA1physical
18850631
THIC_HUMANACAT2physical
22863883
ASNS_HUMANASNSphysical
22863883
HDGF_HUMANHDGFphysical
22863883
MARE1_HUMANMAPRE1physical
22863883
RUXF_HUMANSNRPFphysical
22863883
TRXR1_HUMANTXNRD1physical
22863883
TBG1_HUMANTUBG1physical
24289923
BRCA1_HUMANBRCA1physical
24289923
BARD1_HUMANBARD1physical
24289923
BAP31_HUMANBCAP31physical
26344197
PHB_HUMANPHBphysical
26344197
TBB5_HUMANTUBBphysical
26344197
PRP31_HUMANPRPF31physical
27173435
THOC4_HUMANALYREFphysical
27173435
LSM4_HUMANLSM4physical
27173435
LSM8_HUMANLSM8physical
27173435
RL26L_HUMANRPL26L1physical
27173435
SART3_HUMANSART3physical
27173435
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 OLA1_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-216; LYS-242 AND LYS-294,AND MASS SPECTROMETRY.

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