ITA1_DROME - dbPTM
ITA1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA1_DROME
UniProt AC Q24247
Protein Name Integrin alpha-PS1
Gene Name mew
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1146
Subcellular Localization Apical cell membrane
Single-pass type I membrane protein . Lateral cell membrane
Single-pass type I membrane protein . Basal cell membrane
Single-pass type I membrane protein . During mid-oogenesis, localizes to the apical, to the lateral and t
Protein Description Integrin alpha-PS1/beta-PS is a receptor for laminin..
Protein Sequence MLELPFTTIRPNCRLRQNLGILIILQCVLTCYNFNLEQRLPIVKYGHPHSHFGYSVATHTIGEANGPNKTNCVLVGAPLDQNRQPNTTHSGALWRCPMTQRFDDCEQVITDGRRNFDSEILSPPGNDEIKEDQWMGVTVRSNPLQANGSGGKVIVCAHRYMYIVRENRYGQGLCYLLTNDLQFEEVHEPCKGRPVQRQHEDYGLCQAGTSAALLDDDTMVLGSPGPYTWRGSIWVTQVGGEYLQRDKTTYYSDHSDLNSPVDKYSYLGMSVTGGRFFGHMSYAAGAPRSEGHGQVVIFDKSTDNPIPVHSILDGEQFGSSFGYELATADINGDHRPDLIVAAPLYFTKTEGGAVYVYQNIQDTLPMKYTLKLTGPLESRFGLALANIGDLNKDNCEDLAVGAPYEGNGVVYIYLGSSQGLNSKPAQKIQASELGGTIPNGQPIRTFGISISGNTDLDDNSYPDVVIGAFNSSAAVILLARPIISIQTSVQRKELHNMDPNTPGCLDDPASNLTCFTFRACCSIEPYDEKNKELRLAYSVEAETFDHLKKFSRVFFFDRENKRTNVLSRVVRVHTNGRTECQAVTGYIKANTRDIQTPVRFRLKYSLVEPPLADSALVRLNPILDQTQAHVDFEGTFQKDCGDDDLCESNLIIRVEPNITESSGNEYTLILDETELEVRINVSNLADSAYEAQLFIAHQAGVSYVATKKPTNATCNSYNTTLVACSLGNPMLRDTTTFVTIRFQPKGLEPSEKIMLFHIFANTTSKLVGPERPERDLRVNVVRRAKLNFRGWAIPEQSFYSGSSVANSVANTAATDIEGHGPMGMDDVGSQVHHMFTIFNEGPSTAPKVQMVIHWPYSLYSDPQSGRPVQYLLYLEQVPTVEVSQGECHVAKEYVNPLNLASGSRENPAYLSAPAQMRMFPSQSRHSFNKSLIHSQRSYYSSSHRDDHSDDTQSNRNRVRRSFLERVTRLERLMYDPESSNAANGKKQDIVELDCNKGATNCVRIECDILNMPALSEAQVVVKARLWNSTLVSEYPRVERVRIFSTATAQIPESYGVEVMDHNNIEVETRAYPELRNQQRDTSIPWLIIILGIVGGLLLLALVTYVLWKVGFFKRIRPTDPTLSGNLEKMNEEKPFLAPSKNTHHVF
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
68N-linked_GlycosylationIGEANGPNKTNCVLV
CCCCCCCCCCCEEEE
66.24-
86N-linked_GlycosylationLDQNRQPNTTHSGAL
CCCCCCCCCCCCCEE
49.63-
147N-linked_GlycosylationRSNPLQANGSGGKVI
ECCCEEECCCCCEEE
32.00-
470N-linked_GlycosylationDVVIGAFNSSAAVIL
CEEEEECCCCHHHHH
34.22-
511N-linked_GlycosylationCLDDPASNLTCFTFR
CCCCHHHCCEEEEEE
41.28-
657N-linked_GlycosylationLIIRVEPNITESSGN
EEEEECCCEECCCCC
40.0717893096
680N-linked_GlycosylationTELEVRINVSNLADS
CEEEEEEEHHHHCCC
22.17-
711N-linked_GlycosylationVATKKPTNATCNSYN
EEECCCCCCCCCCCC
41.6019349973
718N-linked_GlycosylationNATCNSYNTTLVACS
CCCCCCCCCEEEEEE
26.8019349973
761N-linked_GlycosylationMLFHIFANTTSKLVG
EEEEEECCCCCCCCC
32.8919349973
928N-linked_GlycosylationSQSRHSFNKSLIHSQ
CCCCCCCCHHHHHHH
35.70-
1027N-linked_GlycosylationVVKARLWNSTLVSEY
EEEEECCCCCCCCCC
29.7017893096

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 ITA1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA1_DROME !!

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 ITA1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITA2_DROMEifgenetic
8674437
ITA2_DROMEifgenetic
9250662
ITA2_DROMEifgenetic
9435290
SLIT_DROMEsligenetic
12040052
SRF_DROMEbsgenetic
9755209
SOG_DROMEsogphysical
12835400

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA1_DROME

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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-711; ASN-718 AND ASN-761,AND MASS SPECTROMETRY.
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657 AND ASN-1027, AND MASSSPECTROMETRY.

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