ANTR2_HUMAN - dbPTM
ANTR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANTR2_HUMAN
UniProt AC P58335
Protein Name Anthrax toxin receptor 2
Gene Name ANTXR2
Organism Homo sapiens (Human).
Sequence Length 489
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein. Expressed at the cell surface.
Isoform 2: Endoplasmic reticulum membrane
Single-pass type I membrane protein. Expressed predominantly within the endoplasmic reticulum and not at th
Protein Description Necessary for cellular interactions with laminin and the extracellular matrix..
Protein Sequence MVAERSPARSPGSWLFPGLWLLVLSGPGGLLRAQEQPSCRRAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQVFPVKGGFQALKGIINSILAQSCTEILELQPSSVCVGEEFQIVLSGRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSVSFNGGKSVISGSLIVTATECSNGIAAIIVILVLLLLLGIGLMWWFWPLCCKVVIKDPPPPPAPAPKEEEEEPLPTKKWPTVDASYYGGRGVGGIKRMEVRWGDKGSTEEGARLEKAKNAVVKIPEETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQEGDEVCIWECIEKELTA
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
81PhosphorylationVSPEMRLSFIVFSSQ
CCHHHEEEEEEECCC		11.5426503514
86PhosphorylationRLSFIVFSSQATIIL
EEEEEEECCCCEEEE		15.6226503514
87PhosphorylationLSFIVFSSQATIILP
EEEEEECCCCEEEEE		16.6363750377
90PhosphorylationIVFSSQATIILPLTG
EEECCCCEEEEECCC		10.83113136263
96PhosphorylationATIILPLTGDRGKIS
CEEEEECCCCCCCCC		34.7963750379
113PhosphorylationLEDLKRVSPVGETYI
HHHHHCCCCCCCHHH		20.2123917254
118PhosphorylationRVSPVGETYIHEGLK
CCCCCCCHHHHHHHH		23.1162165707
119PhosphorylationVSPVGETYIHEGLKL
CCCCCCHHHHHHHHH		8.9362165709
147PhosphorylationSSIIIALTDGKLDGL
CEEEEEEECCCCCCC		33.4124260401
161AcetylationLVPSYAEKEAKISRS
CCCCHHHHHHHHHHH		55.5912436323
168PhosphorylationKEAKISRSLGASVYC
HHHHHHHHHCCEEEE		25.1029759185
172PhosphorylationISRSLGASVYCVGVL
HHHHHCCEEEEEEEE		16.3029759185
240PhosphorylationEEFQIVLSGRGFMLG
CEEEEEEECCCEECC		18.6224719451
250N-linked_GlycosylationGFMLGSRNGSVLCTY
CEECCCCCCCEEEEE		49.11UniProtKB CARBOHYD
260N-linked_GlycosylationVLCTYTVNETYTTSV
EEEEEECCCEECCCC		28.26UniProtKB CARBOHYD
268UbiquitinationETYTTSVKPVSVQLN
CEECCCCCEEEEEEC		39.20-
268 (in isoform 2)Ubiquitination-39.2021890473
296 (in isoform 2)Ubiquitination-12.8921890473
340 (in isoform 2)Ubiquitination-2.5821890473
346UbiquitinationWFWPLCCKVVIKDPP
HHHHHHCEEECCCCC		38.24-
346 (in isoform 2)Ubiquitination-38.2421890473
370PhosphorylationEEEEPLPTKKWPTVD
CCCCCCCCCCCCCCC		53.6022964224
371 (in isoform 1)Ubiquitination-51.4021890473
371 (in isoform 4)Ubiquitination-51.4021890473
371UbiquitinationEEEPLPTKKWPTVDA
CCCCCCCCCCCCCCC		51.4021906983
372UbiquitinationEEPLPTKKWPTVDAS
CCCCCCCCCCCCCCH		61.97-
375O-linked_GlycosylationLPTKKWPTVDASYYG
CCCCCCCCCCCHHCC		29.87OGP
375PhosphorylationLPTKKWPTVDASYYG
CCCCCCCCCCCHHCC		29.8721945579
379PhosphorylationKWPTVDASYYGGRGV
CCCCCCCHHCCCCCC		17.9021945579
380PhosphorylationWPTVDASYYGGRGVG
CCCCCCHHCCCCCCC		14.0921945579
381PhosphorylationPTVDASYYGGRGVGG
CCCCCHHCCCCCCCC		15.6021945579
399UbiquitinationMEVRWGDKGSTEEGA
EEEECCCCCCCHHHH		51.3121906983
399 (in isoform 1)Ubiquitination-51.3121890473
399 (in isoform 4)Ubiquitination-51.3121890473
401PhosphorylationVRWGDKGSTEEGARL
EECCCCCCCHHHHHH		38.0828857561
402PhosphorylationRWGDKGSTEEGARLE
ECCCCCCCHHHHHHH		46.8829457462
443 (in isoform 1)Ubiquitination-32.7221890473
443UbiquitinationTHQPPQTKWYTPIKG
CCCCCCCCCCCCCCC		32.7221890473
443 (in isoform 4)Ubiquitination-32.7221890473
445PhosphorylationQPPQTKWYTPIKGRL
CCCCCCCCCCCCCHH		12.2820080640
446PhosphorylationPPQTKWYTPIKGRLD
CCCCCCCCCCCCHHH		19.8822199227
449 (in isoform 1)Ubiquitination-38.9021890473
449UbiquitinationTKWYTPIKGRLDALW
CCCCCCCCCHHHHHH		38.9021890473
449 (in isoform 4)Ubiquitination-38.9021890473
463PhosphorylationWALLRRQYDRVSLMR
HHHHHHCCCCCCCCC		12.1426639799
483 (in isoform 4)Phosphorylation-6.0129978859
487 (in isoform 4)Phosphorylation-7.9125884760
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 ANTR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANTR2_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 ANTR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO4A5_HUMANCOL4A5physical
11683410
LAMB1_HUMANLAMB1physical
11683410
LAMC1_HUMANLAMC1physical
11683410
ELOA1_HUMANTCEB3physical
28514442
H1BP3_HUMANHS1BP3physical
28514442
IKIP_HUMANIKBIPphysical
28514442
AN13D_HUMANANKRD13Dphysical
28514442
Drug and Disease Associations
Kegg Disease
H00614 Infantile systemic hyalinosis and juvenile hyaline fibromatosis
OMIM Disease
228600Hyaline fibromatosis syndrome (HFS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANTR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND MASSSPECTROMETRY.

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