ANTR1_HUMAN - dbPTM
ANTR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANTR1_HUMAN
UniProt AC Q9H6X2
Protein Name Anthrax toxin receptor 1
Gene Name ANTXR1
Organism Homo sapiens (Human).
Sequence Length 564
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, lamellipodium membrane
Single-pass type I membrane protein . Cell projection, filopodium membrane
Single-pass type I membrane protein . At the membrane of lamellipodia and at
Protein Description Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells..
Protein Sequence MATAERRALGIGFQWLSLATLVLICAGQGGRREDGGPACYGGFDLYFILDKSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDTYMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHVFPVNDGFQALQGIIHSILKKSCIEILAAEPSTICAGESFQVVVRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQVSMNDGLSFISSSVIITTTHCSDGSILAIALLILFLLLALALLWWFWPLCCTVIIKEVPPPPAEESEEEDDDGLPKKKWPTVDASYYGGRGVGGIKRMEVRWGEKGSTEEGAKLEKAKNARVKMPEQEYEFPEPRNLNNNMRRPSSPRKWYSPIKGKLDALWVLLRKGYDRVSVMRPQPGDTGRCINFTRVKNNQPAKYPLNNAYHTSSPPPAPIYTPPPPAPHCPPPPPSAPTPPIPSPPSTLPPPPQAPPPNRAPPPSRPPPRPSV
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-----MATAERRALG
-----CCHHHHHHHC		27.9624719451
17PhosphorylationGIGFQWLSLATLVLI
CCHHHHHHHHHHHHH		17.0122210691
20PhosphorylationFQWLSLATLVLICAG
HHHHHHHHHHHHHHC		23.7722210691
75PhosphorylationQLAHKFISPQLRMSF
HHHHHHCCHHHCCEE		15.1024719451
81PhosphorylationISPQLRMSFIVFSTR
CCHHHCCEEEEEECC		12.8520068231
86PhosphorylationRMSFIVFSTRGTTLM
CCEEEEEECCCCEEE		13.2920068231
87PhosphorylationMSFIVFSTRGTTLMK
CEEEEEECCCCEEEH		22.9620068231
90PhosphorylationIVFSTRGTTLMKLTE
EEEECCCCEEEHHHH		17.2920068231
91PhosphorylationVFSTRGTTLMKLTED
EEECCCCEEEHHHHC		27.9020068231
119PhosphorylationVLPGGDTYMHEGFER
HCCCCCCCCCCCHHH		10.9511265487
132PhosphorylationERASEQIYYENRQGY
HHHHHHHHEECCCCC		12.3811265497
133PhosphorylationRASEQIYYENRQGYR
HHHHHHHEECCCCCC		14.3511265507
139PhosphorylationYYENRQGYRTASVII
HEECCCCCCEEEEEE		9.107840285
166N-linked_GlycosylationFYSEREANRSRDLGA
ECCHHHHHHCCCCEE		37.39UniProtKB CARBOHYD
184N-linked_GlycosylationCVGVKDFNETQLARI
EEECCCCCHHHHHHH		62.6319349973
184N-linked_GlycosylationCVGVKDFNETQLARI
EEECCCCCHHHHHHH		62.6319349973
195UbiquitinationLARIADSKDHVFPVN
HHHHHCCCCCEEECC		53.02-
214PhosphorylationALQGIIHSILKKSCI
HHHHHHHHHHHHHHH		21.1424719451
262N-linked_GlycosylationVLCSFKINDSVTLNE
EEEEEEECCCEECCC		35.77UniProtKB CARBOHYD
262N-linked_GlycosylationVLCSFKINDSVTLNE
EEEEEEECCCEECCC		35.7719349973
270UbiquitinationDSVTLNEKPFSVEDT
CCEECCCCCCCCCCC		50.73-
298 (in isoform 4)Phosphorylation-10.0224043423
304 (in isoform 4)Phosphorylation-26.5124043423
307 (in isoform 4)Phosphorylation-17.9824043423
308 (in isoform 4)Phosphorylation-24.6524043423
309 (in isoform 4)Phosphorylation-15.5624043423
313 (in isoform 4)Phosphorylation-17.9624043423
314 (in isoform 4)Phosphorylation-12.2524043423
315 (in isoform 4)Phosphorylation-16.5424043423
318 (in isoform 4)Phosphorylation-37.0824043423
347S-palmitoylationWWFWPLCCTVIIKEV
HHHHHHHHHHHHHHC		4.4816401723
362PhosphorylationPPPPAEESEEEDDDG
CCCCCCCCCCCCCCC		41.6429255136
374UbiquitinationDDGLPKKKWPTVDAS
CCCCCCCCCCCCCCH		65.61-
377PhosphorylationLPKKKWPTVDASYYG
CCCCCCCCCCCHHCC		29.8721945579
381PhosphorylationKWPTVDASYYGGRGV
CCCCCCCHHCCCCCC		17.9021945579
382PhosphorylationWPTVDASYYGGRGVG
CCCCCCHHCCCCCCC		14.0921945579
383PhosphorylationPTVDASYYGGRGVGG
CCCCCHHCCCCCCCC		15.6021945579
401UbiquitinationMEVRWGEKGSTEEGA
EEECCCCCCCCHHHH		54.98-
403PhosphorylationVRWGEKGSTEEGAKL
ECCCCCCCCHHHHHH		43.6525002506
404PhosphorylationRWGEKGSTEEGAKLE
CCCCCCCCHHHHHHH		46.8825002506
409UbiquitinationGSTEEGAKLEKAKNA
CCCHHHHHHHHHHHC		68.95-
419UbiquitinationKAKNARVKMPEQEYE
HHHHCCCCCCHHHCC		43.0921906983
419 (in isoform 1)Ubiquitination-43.0921890473
425PhosphorylationVKMPEQEYEFPEPRN
CCCCHHHCCCCCCCC		23.6721945579
441PhosphorylationNNNMRRPSSPRKWYS
CCCCCCCCCCCCCCC		51.6820068231
442PhosphorylationNNMRRPSSPRKWYSP
CCCCCCCCCCCCCCC		31.2630576142
445 (in isoform 1)Ubiquitination-54.6021890473
445UbiquitinationRRPSSPRKWYSPIKG
CCCCCCCCCCCCCCC		54.6021890473
447PhosphorylationPSSPRKWYSPIKGKL
CCCCCCCCCCCCCHH		13.9627134283
448PhosphorylationSSPRKWYSPIKGKLD
CCCCCCCCCCCCHHH		21.0227134283
451UbiquitinationRKWYSPIKGKLDALW
CCCCCCCCCHHHHHH		54.07-
453 (in isoform 1)Ubiquitination-37.8921890473
453UbiquitinationWYSPIKGKLDALWVL
CCCCCCCHHHHHHHH		37.8921890473
481S-palmitoylationQPGDTGRCINFTRVK
CCCCCCCEEEEEEEE		2.9329575903
488UbiquitinationCINFTRVKNNQPAKY
EEEEEEEECCCCCCC		47.06-
501PhosphorylationKYPLNNAYHTSSPPP
CCCCCCCCCCCCCCC		14.0446164567
503PhosphorylationPLNNAYHTSSPPPAP
CCCCCCCCCCCCCCC		20.4446164561
521S-palmitoylationPPPPAPHCPPPPPSA
CCCCCCCCCCCCCCC		5.4316401723
556PhosphorylationPNRAPPPSRPPPRPS
CCCCCCCCCCCCCCC		64.2929255136
563PhosphorylationSRPPPRPSV------
CCCCCCCCC------		41.5630266825
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 ANTR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANTR1_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 ANTR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB3_HUMANTUBB3physical
26186194
RSAD1_HUMANRSAD1physical
26186194
CAH11_HUMANCA11physical
26186194
OZF_HUMANZNF146physical
26186194
POTEF_HUMANPOTEFphysical
26186194
TBB8_HUMANTUBB8physical
26186194
GRP78_HUMANHSPA5physical
26186194
KANK2_HUMANKANK2physical
26186194
RICTR_HUMANRICTORphysical
26186194
LRP11_HUMANLRP11physical
26186194
PDIA5_HUMANPDIA5physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
PYC_HUMANPCphysical
26186194
DJC12_HUMANDNAJC12physical
26186194
OBSL1_HUMANOBSL1physical
26186194
RL23_HUMANRPL23physical
26186194
G6PE_HUMANH6PDphysical
26186194
KIRR1_HUMANKIRRELphysical
26186194
GALT7_HUMANGALNT7physical
26186194
WFS1_HUMANWFS1physical
26186194
PCYOX_HUMANPCYOX1physical
26186194
CNTP3_HUMANCNTNAP3physical
26186194
FOXF2_HUMANFOXF2physical
26186194
TBB4A_HUMANTUBB4Aphysical
26186194
DMXL2_HUMANDMXL2physical
26186194
MP2K7_HUMANMAP2K7physical
26186194
ETV3_HUMANETV3physical
26186194
MANEA_HUMANMANEAphysical
26186194
ERF_HUMANERFphysical
26186194
TRM44_HUMANTRMT44physical
26186194
TIM16_HUMANPAM16physical
26186194
GDF11_HUMANGDF11physical
26186194
SAMD1_HUMANSAMD1physical
26186194
WNT5A_HUMANWNT5Aphysical
26186194
G6PE_HUMANH6PDphysical
28514442
DJC12_HUMANDNAJC12physical
28514442
PDIA5_HUMANPDIA5physical
28514442
CAH11_HUMANCA11physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
OBSL1_HUMANOBSL1physical
28514442
B4GN4_HUMANB4GALNT4physical
28514442
FOXF2_HUMANFOXF2physical
28514442
CNTP3_HUMANCNTNAP3physical
28514442
KIRR1_HUMANKIRRELphysical
28514442
TBB8_HUMANTUBB8physical
28514442
RICTR_HUMANRICTORphysical
28514442
PCYOX_HUMANPCYOX1physical
28514442
WNT5A_HUMANWNT5Aphysical
28514442
POTEF_HUMANPOTEFphysical
28514442
MP2K7_HUMANMAP2K7physical
28514442
GRP78_HUMANHSPA5physical
28514442
SAMD1_HUMANSAMD1physical
28514442
MANEA_HUMANMANEAphysical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
PYC_HUMANPCphysical
28514442
RL23_HUMANRPL23physical
28514442
DMXL2_HUMANDMXL2physical
28514442
GALT7_HUMANGALNT7physical
28514442
WFS1_HUMANWFS1physical
28514442
ERF_HUMANERFphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602089Hemangioma, capillary infantile (HCI)
230740GAPO syndrome (GAPO)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANTR1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-425, AND MASSSPECTROMETRY.

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