ITAM_HUMAN - dbPTM
ITAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITAM_HUMAN
UniProt AC P11215
Protein Name Integrin alpha-M
Gene Name ITGAM
Organism Homo sapiens (Human).
Sequence Length 1152
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Membrane raft
Single-pass type I membrane protein .
Protein Description Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. [PubMed: 28807980 In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils]
Protein Sequence MALRVLLLTALTLCHGFNLDTENAMTFQENARGFGQSVVQLQGSRVVVGAPQEIVAANQRGSLYQCDYSTGSCEPIRLQVPVEAVNMSLGLSLAATTSPPQLLACGPTVHQTCSENTYVKGLCFLFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEALKTIQNQLREKIFAIEGTQTGSSSSFEHEMSQEGFSAAITSNGPLLSTVGSYDWAGGVFLYTSKEKSTFINMTRVDSDMNDAYLGYAAAIILRNRVQSLVLGAPRYQHIGLVAMFRQNTGMWESNANVKGTQIGAYFGASLCSVDVDSNGSTDLVLIGAPHYYEQTRGGQVSVCPLPRGRARWQCDAVLYGEQGQPWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNRGAVYLFHGTSGSGISPSHSQRIAGSKLSPRLQYFGQSLSGGQDLTMDGLVDLTVGAQGHVLLLRSQPVLRVKAIMEFNPREVARNVFECNDQVVKGKEAGEVRVCLHVQKSTRDRLREGQIQSVVTYDLALDSGRPHSRAVFNETKNSTRRQTQVLGLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPLSAFGNLRPVLAEDAQRLFTALFPFEKNCGNDNICQDDLSITFSFMSLDCLVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSQRSWRLACESASSTEVSGALKSTSCSINHPIFPENSEVTFNITFDVDSKASLGNKLLLKANVTSENNMPRTNKTEFQLELPVKYAVYMVVTSHGVSTKYLNFTASENTSRVMQHQYQVSNLGQRSLPISLVFLVPVRLNQTVIWDRPQVTFSENLSSTCHTKERLPSHSDFLAELRKAPVVNCSIAVCQRIQCDIPFFGIQEEFNATLKGNLSFDWYIKTSHNHLLIVSTAEILFNDSVFTLLPGQGAFVRSQTETKVEPFEVPNPLPLIVGSSVGGLLLLALITAALYKLGFFKRQYKDMMSEGGPPGAEPQ
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
86N-linked_GlycosylationQVPVEAVNMSLGLSL
ECCHHHEEHHHCCEE		22.75UniProtKB CARBOHYD
213PhosphorylationQNNPNPRSLVKPITQ
CCCCCHHHHHHHHHH		38.4826356563
219PhosphorylationRSLVKPITQLLGRTH
HHHHHHHHHHHCCCC		22.9926356563
240N-linked_GlycosylationKVVRELFNITNGARK
HHHHHHHHCCCCCCC		53.45UniProtKB CARBOHYD
240N-linked_GlycosylationKVVRELFNITNGARK
HHHHHHHHCCCCCCC		53.4517623646
242PhosphorylationVRELFNITNGARKNA
HHHHHHCCCCCCCCC		28.8022985185
283PhosphorylationDREGVIRYVIGVGDA
HCCCCCEEEEECHHH		5.8228555341
338PhosphorylationKIFAIEGTQTGSSSS
CEEEEECCCCCCCCC		15.3528787133
342PhosphorylationIEGTQTGSSSSFEHE
EECCCCCCCCCCEEE		30.3628787133
351PhosphorylationSSFEHEMSQEGFSAA
CCCEEECCCCCCCEE		23.3028787133
391N-linked_GlycosylationKEKSTFINMTRVDSD
CCCCCEEEEEECCCC		22.91UniProtKB CARBOHYD
418PhosphorylationILRNRVQSLVLGAPR
HHHHHHHHHHHCCCC		20.0027174698
426PhosphorylationLVLGAPRYQHIGLVA
HHHCCCCCCEEEEEE		11.9027174698
469N-linked_GlycosylationCSVDVDSNGSTDLVL
EEEECCCCCCEEEEE		43.93UniProtKB CARBOHYD
574PhosphorylationHSQRIAGSKLSPRLQ
HHHHCCCCCCCHHHH		22.7719664994
577PhosphorylationRIAGSKLSPRLQYFG
HCCCCCCCHHHHHHC		16.2319664994
676PhosphorylationQIQSVVTYDLALDSG
CCCEEEEEEEECCCC		9.43-
692N-linked_GlycosylationPHSRAVFNETKNSTR
CCHHHHHCCCCCCCH		49.80UniProtKB CARBOHYD
696N-linked_GlycosylationAVFNETKNSTRRQTQ
HHHCCCCCCCHHHHH		56.91UniProtKB CARBOHYD
734N-linked_GlycosylationSPIVLRLNFSLVGTP
CCEEEEECEEEECCC		20.30UniProtKB CARBOHYD
801N-linked_GlycosylationVGGPREFNVTVTVRN
ECCCCEEEEEEEEEC		24.65UniProtKB CARBOHYD
805PhosphorylationREFNVTVTVRNDGED
CEEEEEEEEECCCCC		12.37-
833PhosphorylationLSYRKVSTLQNQRSQ
CCCEEHHHHHHHHHH		35.0423403867
839PhosphorylationSTLQNQRSQRSWRLA
HHHHHHHHHHHHHHH		21.8523403867
851PhosphorylationRLACESASSTEVSGA
HHHHCCCCCCCCCCC		47.2628450419
852PhosphorylationLACESASSTEVSGAL
HHHCCCCCCCCCCCC		28.4428450419
853PhosphorylationACESASSTEVSGALK
HHCCCCCCCCCCCCC		37.6028450419
856PhosphorylationSASSTEVSGALKSTS
CCCCCCCCCCCCCCC		16.4728450419
880N-linked_GlycosylationENSEVTFNITFDVDS
CCCEEEEEEEEECCC		24.03UniProtKB CARBOHYD
900N-linked_GlycosylationNKLLLKANVTSENNM
CEEEEEECCCCCCCC		35.6919159218
911N-linked_GlycosylationENNMPRTNKTEFQLE
CCCCCCCCCCEEEEE		51.00UniProtKB CARBOHYD
930PhosphorylationYAVYMVVTSHGVSTK
EEEEEEEECCCCCCE		12.00-
931PhosphorylationAVYMVVTSHGVSTKY
EEEEEEECCCCCCEE		13.46-
940N-linked_GlycosylationGVSTKYLNFTASENT
CCCCEEEEEECCCCH		29.1819159218
946N-linked_GlycosylationLNFTASENTSRVMQH
EEEECCCCHHHHHHH		40.6419159218
978N-linked_GlycosylationFLVPVRLNQTVIWDR
EEEEEECCCEEEECC		25.55UniProtKB CARBOHYD
993N-linked_GlycosylationPQVTFSENLSSTCHT
CCEECCCCCCCCCCC		43.98UniProtKB CARBOHYD
1021N-linked_GlycosylationLRKAPVVNCSIAVCQ
HHCCCCCCEEEEECC		17.66UniProtKB CARBOHYD
1044N-linked_GlycosylationFGIQEEFNATLKGNL
CCCHHHCCEEECCCC		34.98UniProtKB CARBOHYD
1050N-linked_GlycosylationFNATLKGNLSFDWYI
CCEEECCCCCEEEEE		30.81UniProtKB CARBOHYD
1075N-linked_GlycosylationSTAEILFNDSVFTLL
ECEEEHHCCCCHHCC		36.88UniProtKB CARBOHYD
1142PhosphorylationRQYKDMMSEGGPPGA
HHHHHHHHCCCCCCC		26.8416857989
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 ITAM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITAM_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 ITAM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRAK1_HUMANIRAK1physical
11701612
ICAM1_HUMANICAM1physical
12208882
JAM3_HUMANJAM3physical
12208882
BAP31_HUMANBCAP31physical
15294914
SHRPN_HUMANSHARPINphysical
24210817
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609939Systemic lupus erythematosus 6 (SLEB6)
Kegg Drug
D08993 Rovelizumab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITAM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-900; ASN-940 AND ASN-946,AND MASS SPECTROMETRY.

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