ANGP4_HUMAN - dbPTM
ANGP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANGP4_HUMAN
UniProt AC Q9Y264
Protein Name Angiopoietin-4
Gene Name ANGPT4
Organism Homo sapiens (Human).
Sequence Length 503
Subcellular Localization Secreted .
Protein Description Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis..
Protein Sequence MLSQLAMLQGSLLLVVATMSVAQQTRQEADRGCETLVVQHGHCSYTFLLPKSEPCPPGPEVSRDSNTLQRESLANPLHLGKLPTQQVKQLEQALQNNTQWLKKLERAIKTILRSKLEQVQQQMAQNQTAPMLELGTSLLNQTTAQIRKLTDMEAQLLNQTSRMDAQMPETFLSTNKLENQLLLQRQKLQQLQGQNSALEKRLQALETKQQEELASILSKKAKLLNTLSRQSAALTNIERGLRGVRHNSSLLQDQQHSLRQLLVLLRHLVQERANASAPAFIMAGEQVFQDCAEIQRSGASASGVYTIQVSNATKPRKVFCDLQSSGGRWTLIQRRENGTVNFQRNWKDYKQGFGDPAGEHWLGNEVVHQLTRRAAYSLRVELQDWEGHEAYAQYEHFHLGSENQLYRLSVVGYSGSAGRQSSLVLQNTSFSTLDSDNDHCLCKCAQVMSGGWWFDACGLSNLNGVYYHAPDNKYKMDGIRWHYFKGPSYSLRASRMMIRPLDI
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
3Phosphorylation-----MLSQLAMLQG
-----CHHHHHHHHH
23.1124043423
11PhosphorylationQLAMLQGSLLLVVAT
HHHHHHHHHHHHHHH
11.6824043423
18PhosphorylationSLLLVVATMSVAQQT
HHHHHHHHHHHHHHH
9.8124043423
20PhosphorylationLLVVATMSVAQQTRQ
HHHHHHHHHHHHHHH
15.2224043423
25PhosphorylationTMSVAQQTRQEADRG
HHHHHHHHHHHHHCC
23.4124043423
72PhosphorylationSNTLQRESLANPLHL
CCCCCHHHCCCCHHH
34.6646163225
96N-linked_GlycosylationQLEQALQNNTQWLKK
HHHHHHHHCHHHHHH
55.13UniProtKB CARBOHYD
126N-linked_GlycosylationVQQQMAQNQTAPMLE
HHHHHHHCCCHHHHH
31.47UniProtKB CARBOHYD
140N-linked_GlycosylationELGTSLLNQTTAQIR
HHHHHHHHHHHHHHH
42.31UniProtKB CARBOHYD
150PhosphorylationTAQIRKLTDMEAQLL
HHHHHHHHHHHHHHH
36.0146163231
158N-linked_GlycosylationDMEAQLLNQTSRMDA
HHHHHHHHHHCCHHC
52.23UniProtKB CARBOHYD
215PhosphorylationKQQEELASILSKKAK
HHHHHHHHHHHHHHH
36.3724719451
226PhosphorylationKKAKLLNTLSRQSAA
HHHHHHHHHHHHHHH
26.5346163237
228PhosphorylationAKLLNTLSRQSAALT
HHHHHHHHHHHHHHH
26.6646163221
247N-linked_GlycosylationGLRGVRHNSSLLQDQ
HHHHHHCCHHHHHHH
23.80UniProtKB CARBOHYD
248PhosphorylationLRGVRHNSSLLQDQQ
HHHHHCCHHHHHHHH
19.0822817900
249PhosphorylationRGVRHNSSLLQDQQH
HHHHCCHHHHHHHHH
38.1122817900
274N-linked_GlycosylationHLVQERANASAPAFI
HHHHHHHHCCCCCCH
40.42UniProtKB CARBOHYD
311N-linked_GlycosylationVYTIQVSNATKPRKV
EEEEEEECCCCCCEE
53.42UniProtKB CARBOHYD
324PhosphorylationKVFCDLQSSGGRWTL
EEEEEECCCCCCEEE
37.9425954137
337N-linked_GlycosylationTLIQRRENGTVNFQR
EEEEEECCCCCCEEE
50.01UniProtKB CARBOHYD
377PhosphorylationLTRRAAYSLRVELQD
HHHHHHHHEEEEEEC
12.6524719451
427N-linked_GlycosylationQSSLVLQNTSFSTLD
CCCEEEECCCCCCCC
33.26UniProtKB CARBOHYD
490PhosphorylationYFKGPSYSLRASRMM
EECCCCCCHHHHHEE
18.7324719451

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 ANGP4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANGP4_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 ANGP4_HUMAN !!

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

Oops, there are no PPI records of ANGP4_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 ANGP4_HUMAN

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Related Literatures of Post-Translational Modification

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