ANGE1_HUMAN - dbPTM
ANGE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANGE1_HUMAN
UniProt AC Q9UNK9
Protein Name Protein angel homolog 1
Gene Name ANGEL1
Organism Homo sapiens (Human).
Sequence Length 670
Subcellular Localization
Protein Description
Protein Sequence MIASCLCYLLLPATRLFRALSDAFFTCRKNVLLANSSSPQVEGDFAMAPRGPEQEECEGLLQQWREEGLSQVLSTASEGPLIDKGLAQSSLALLMDNPGEENAASEDRWSSRQLSDLRAAENLDEPFPEMLGEEPLLEVEGVEGSMWAAIPMQSEPQYADCAALPVGALATEQWEEDPAVLAWSIAPEPVPQEEASIWPFEGLGQLQPPAVEIPYHEILWREWEDFSTQPDAQGLKAGDGPQFQFTLMSYNILAQDLMQQSSELYLHCHPDILNWNYRFVNLMQEFQHWDPDILCLQEVQEDHYWEQLEPSLRMMGFTCFYKRRTGCKTDGCAVCYKPTRFRLLCASPVEYFRPGLELLNRDNVGLVLLLQPLVPEGLGQVSVAPLCVANTHILYNPRRGDVKLAQMAILLAEVDKVARLSDGSHCPIILCGDLNSVPDSPLYNFIRDGELQYHGMPAWKVSGQEDFSHQLYQRKLQAPLWPSSLGITDCCQYVTSCHPKRSERRKYGRDFLLRFRFCSIACQRPVGLVLMEGVTDTKPERPAGWAESVLEEDASELEPAFSRTVGTIQHCLHLTSVYTHFLPQRGRPEVTTMPLGLGMTVDYIFFSAESCENGNRTDHRLYRDGTLKLLGRLSLLSEEILWAANGLPNPFCSSDHLCLLASFGMEVTAP
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
5S-palmitoylation---MIASCLCYLLLP
---CHHHHHHHHHHH
1.9429575903
7S-palmitoylation-MIASCLCYLLLPAT
-CHHHHHHHHHHHHH
2.3629575903
29UbiquitinationDAFFTCRKNVLLANS
HHHHHHHCCEEECCC
54.2621906983
36PhosphorylationKNVLLANSSSPQVEG
CCEEECCCCCCCCCC
26.9626657352
37PhosphorylationNVLLANSSSPQVEGD
CEEECCCCCCCCCCC
45.9330108239
38PhosphorylationVLLANSSSPQVEGDF
EEECCCCCCCCCCCE
21.1225159151
70PhosphorylationQWREEGLSQVLSTAS
HHHHHCHHHHHHHCC
29.1521712546
77PhosphorylationSQVLSTASEGPLIDK
HHHHHHCCCCCCCCH
43.08-
105PhosphorylationPGEENAASEDRWSSR
CCCCCCCCCCCCCHH
37.3028348404
110PhosphorylationAASEDRWSSRQLSDL
CCCCCCCCHHHHHHH
19.2828348404
111PhosphorylationASEDRWSSRQLSDLR
CCCCCCCHHHHHHHH
19.6528348404
115PhosphorylationRWSSRQLSDLRAAEN
CCCHHHHHHHHHHHC
26.6824719451
318PhosphorylationSLRMMGFTCFYKRRT
HHHHCCCEEEEECCC
8.9346163179
328UbiquitinationYKRRTGCKTDGCAVC
EECCCCCCCCCCEEE
51.50-
336PhosphorylationTDGCAVCYKPTRFRL
CCCCEEEECCCCEEE
17.2611079431
337UbiquitinationDGCAVCYKPTRFRLL
CCCEEEECCCCEEEE
34.48-
347PhosphorylationRFRLLCASPVEYFRP
CEEEEECCCHHHHCC
28.6072500113
351PhosphorylationLCASPVEYFRPGLEL
EECCCHHHHCCCHHH
12.7272500119
416UbiquitinationILLAEVDKVARLSDG
HHHHHHHHHHCCCCC
42.86-
460UbiquitinationYHGMPAWKVSGQEDF
ECCCCCEEECCCCCC
28.73-
472PhosphorylationEDFSHQLYQRKLQAP
CCCHHHHHHHHCCCC
10.3325159151
475UbiquitinationSHQLYQRKLQAPLWP
HHHHHHHHCCCCCCC
29.44-
591PhosphorylationQRGRPEVTTMPLGLG
CCCCCCCCCCCCCCC
18.7322210691
592PhosphorylationRGRPEVTTMPLGLGM
CCCCCCCCCCCCCCC
23.2022210691
622PhosphorylationNRTDHRLYRDGTLKL
CCCCCEEHHHHHHHH
13.4522817900
628UbiquitinationLYRDGTLKLLGRLSL
EHHHHHHHHHHHHHH
41.31-

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 ANGE1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANGE1_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 ANGE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ANGE1_HUMAN !!

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 ANGE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND TYR-351, ANDMASS SPECTROMETRY.

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