APOL2_HUMAN - dbPTM
APOL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APOL2_HUMAN
UniProt AC Q9BQE5
Protein Name Apolipoprotein L2
Gene Name APOL2
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Cytoplasm .
Protein Description May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles..
Protein Sequence MNPESSIFIEDYLKYFQDQVSRENLLQLLTDDEAWNGFVAAAELPRDEADELRKALNKLASHMVMKDKNRHDKDQQHRQWFLKEFPRLKRELEDHIRKLRALAEEVEQVHRGTTIANVVSNSVGTTSGILTLLGLGLAPFTEGISFVLLDTGMGLGAAAAVAGITCSVVELVNKLRARAQARNLDQSGTNVAKVMKEFVGGNTPNVLTLVDNWYQVTQGIGRNIRAIRRARANPQLGAYAPPPHIIGRISAEGGEQVERVVEGPAQAMSRGTMIVGAATGGILLLLDVVSLAYESKHLLEGAKSESAEELKKRAQELEGKLNFLTKIHEMLQPGQDQ
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
1Acetylation-------MNPESSIF
-------CCHHHHHC
19.94-
58UbiquitinationELRKALNKLASHMVM
HHHHHHHHHHHHHHH
46.40-
66UbiquitinationLASHMVMKDKNRHDK
HHHHHHHCCCCCCCH
54.89-
73MethylationKDKNRHDKDQQHRQW
CCCCCCCHHHHHHHH
51.84-
83UbiquitinationQHRQWFLKEFPRLKR
HHHHHHHHHCHHHHH
48.0821890473
187PhosphorylationQARNLDQSGTNVAKV
HHCCCCCCCCHHHHH
47.4528857561
193UbiquitinationQSGTNVAKVMKEFVG
CCCCHHHHHHHHHHC
38.2821890473
196UbiquitinationTNVAKVMKEFVGGNT
CHHHHHHHHHHCCCC
51.49-
203PhosphorylationKEFVGGNTPNVLTLV
HHHHCCCCCCCEEHH
21.3727251275
239PhosphorylationANPQLGAYAPPPHII
CCCCCCCCCCCCCEE
20.17-
250PhosphorylationPHIIGRISAEGGEQV
CCEEEEEECCCCCCE
20.9325159151
268SulfoxidationVEGPAQAMSRGTMIV
HCCHHHHHHCCCEEE
1.5421406390
269PhosphorylationEGPAQAMSRGTMIVG
CCHHHHHHCCCEEEE
30.4920071362
272PhosphorylationAQAMSRGTMIVGAAT
HHHHHCCCEEEEECH
11.5622210691
279PhosphorylationTMIVGAATGGILLLL
CEEEEECHHHHHHHH
35.0922210691
303UbiquitinationKHLLEGAKSESAEEL
HHHHCCCCCCCHHHH
66.66-
303AcetylationKHLLEGAKSESAEEL
HHHHCCCCCCCHHHH
66.6623236377
304PhosphorylationHLLEGAKSESAEELK
HHHCCCCCCCHHHHH
35.9322210691
306PhosphorylationLEGAKSESAEELKKR
HCCCCCCCHHHHHHH
48.3322210691
3202-HydroxyisobutyrylationRAQELEGKLNFLTKI
HHHHHHHHHHHHHHH
30.77-
320UbiquitinationRAQELEGKLNFLTKI
HHHHHHHHHHHHHHH
30.7721890473
326UbiquitinationGKLNFLTKIHEMLQP
HHHHHHHHHHHHHCC
44.1821890473
330SulfoxidationFLTKIHEMLQPGQDQ
HHHHHHHHHCCCCCC
2.3221406390

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 APOL2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APOL2_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 APOL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBB_HUMANUBBphysical
26186194
BASI_HUMANBSGphysical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
RTL8C_HUMANFAM127Aphysical
26496610
MAST3_HUMANMAST3physical
26496610
RT09_HUMANMRPS9physical
26496610
BPNT1_HUMANBPNT1physical
28514442
UBB_HUMANUBBphysical
28514442
SODC_HUMANSOD1physical
28514442

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 APOL2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-250, AND MASSSPECTROMETRY.
"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-250, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.

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