ITA3_HUMAN - dbPTM
ITA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA3_HUMAN
UniProt AC P26006
Protein Name Integrin alpha-3
Gene Name ITGA3
Organism Homo sapiens (Human).
Sequence Length 1051
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell membrane
Lipid-anchor . Cell projection, invadopodium membrane
Single-pass type I membrane protein . Cell projection, filopodium membrane
Single-pass type I membrane protein . Enriched
Protein Description Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration..
Protein Sequence MGPGPSRAPRAPRLMLCALALMVAAGGCVVSAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRELAVPDGYTNRTGAVYLCPLTAHKDDCERMNITVKNDPGHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDSSDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKEWDLSEYSYKDPEDQGNLYIGYTMQVGSFILHPKNITIVTGAPRHRHMGAVFLLSQEAGGDLRRRQVLEGSQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYVFMNQAGTSFPAHPSLLLHGPSGSAFGLSVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSKGLLRQPQQVIHGEKLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDHIVLLRARPVINIVHKTLVPRPAVLDPALCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLRFAGSESAVFHGFFSMPEMRCQKLELLLMDNLRDKLRPIIISMNYSLPLRMPDRPRLGLRSLDAYPILNQAQALENHTEVQFQKECGPDNKCESNLQMRAAFVSEQQQKLSRLQYSRDVRKLLLSINVTNTRTSERSGEDAHEALLTLVVPPALLLSSVRPPGACQANETIFCELGNPFKRNQRMELLIAFEVIGVTLHTRDLQVQLQLSTSSHQDNLWPMILTLLVDYTLQTSLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLVGLGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWPCRPPGDLINPLNLTLSDPGDRPSSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSETVLTCATGRAHCVWLECPIPDAPVVTNVTVKARVWNSTFIEDYRDFDRVRVNGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY
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
6Phosphorylation--MGPGPSRAPRAPR
--CCCCCCCCCCHHH		47.17-
43UbiquitinationDTRFLVVKEAGNPGS
CCCEEEEEECCCCCC		34.07-
68PhosphorylationQTERQQRYLLLAGAP
CCHHHHHHHHHCCCC		9.4328152594
86N-linked_GlycosylationAVPDGYTNRTGAVYL
CCCCCCCCCCCCEEE		30.91UniProtKB CARBOHYD
107N-linked_GlycosylationKDDCERMNITVKNDP
HHHHHHCCEEECCCC		32.76UniProtKB CARBOHYD
150PhosphorylationRYTQVLWSGSEDQRR
ECEEEEECCCHHHHH		28.42-
1612-HydroxyisobutyrylationDQRRMVGKCYVRGND
HHHHEEEEEEECCCC		15.81-
161UbiquitinationDQRRMVGKCYVRGND
HHHHEEEEEEECCCC		15.81-
2302-HydroxyisobutyrylationNSYMIQRKEWDLSEY
CEEEEEECEECHHHC		46.94-
237PhosphorylationKEWDLSEYSYKDPED
CEECHHHCCCCCHHH		17.58-
238PhosphorylationEWDLSEYSYKDPEDQ
EECHHHCCCCCHHHC		22.96-
265N-linked_GlycosylationSFILHPKNITIVTGA
CEEECCCCEEEEECC		40.88UniProtKB CARBOHYD
267PhosphorylationILHPKNITIVTGAPR
EECCCCEEEEECCCC		20.84-
400PhosphorylationFEGLGKVYIYHSSSK
CCCCCCEEEEECCCC		10.1528152594
402PhosphorylationGLGKVYIYHSSSKGL
CCCCEEEEECCCCCC		4.3028152594
404PhosphorylationGKVYIYHSSSKGLLR
CCEEEEECCCCCCCC		21.2428152594
405PhosphorylationKVYIYHSSSKGLLRQ
CEEEEECCCCCCCCC		23.8228152594
406PhosphorylationVYIYHSSSKGLLRQP
EEEEECCCCCCCCCC		33.4828152594
407UbiquitinationYIYHSSSKGLLRQPQ
EEEECCCCCCCCCCE		56.37-
4072-HydroxyisobutyrylationYIYHSSSKGLLRQPQ
EEEECCCCCCCCCCE		56.37-
471UbiquitinationPVINIVHKTLVPRPA
CCEEEECCCCCCCCC		32.43-
500N-linked_GlycosylationVELCFAYNQSAGNPN
EEHHHHCCCCCCCCC		26.38UniProtKB CARBOHYD
511N-linked_GlycosylationGNPNYRRNITLAYTL
CCCCHHCCEEEEEEE		23.69UniProtKB CARBOHYD
517PhosphorylationRNITLAYTLEADRDR
CCEEEEEEEECCCCC		16.7128555341
571PhosphorylationKLRPIIISMNYSLPL
HCHHEEEEECCCCCC		7.2023684312
573N-linked_GlycosylationRPIIISMNYSLPLRM
HHEEEEECCCCCCCC		19.22UniProtKB CARBOHYD
574PhosphorylationPIIISMNYSLPLRMP
HEEEEECCCCCCCCC		11.7122817900
575PhosphorylationIIISMNYSLPLRMPD
EEEEECCCCCCCCCC		20.6423684312
605N-linked_GlycosylationNQAQALENHTEVQFQ
CHHHHHHCCCEEEEE		48.51UniProtKB CARBOHYD
633PhosphorylationQMRAAFVSEQQQKLS
HHHHHHCCHHHHHHH		24.2029449344
638UbiquitinationFVSEQQQKLSRLQYS
HCCHHHHHHHHCCCC		44.05-
638 (in isoform 1)Ubiquitination-44.0521906983
638 (in isoform 2)Ubiquitination-44.0521906983
656N-linked_GlycosylationRKLLLSINVTNTRTS
HHHHHEEECCCCCCC		31.05UniProtKB CARBOHYD
686PhosphorylationVPPALLLSSVRPPGA
HCHHHHHHCCCCCCC		27.1024719451
697N-linked_GlycosylationPPGACQANETIFCEL
CCCCCCCCCCEEEEC		22.52UniProtKB CARBOHYD
793PhosphorylationKTVEDVGSPLKYEFQ
EEHHHCCCCCEEEEE		27.2323532336
841N-linked_GlycosylationTEITVHGNGSWPCRP
CEEEEECCCCCCCCC		26.84UniProtKB CARBOHYD
857N-linked_GlycosylationGDLINPLNLTLSDPG
CCCCCCCCCCCCCCC		32.03UniProtKB CARBOHYD
861PhosphorylationNPLNLTLSDPGDRPS
CCCCCCCCCCCCCCC		36.2022210691
868PhosphorylationSDPGDRPSSPQRRRR
CCCCCCCCCHHHHHH		56.3922210691
869PhosphorylationDPGDRPSSPQRRRRQ
CCCCCCCCHHHHHHC		27.9522210691
894 (in isoform 2)Ubiquitination-48.8421906983
894 (in isoform 1)Ubiquitination-48.8421906983
894UbiquitinationPVTLAAAKKAKSETV
CCCHHHHHHCCCCCE		48.84-
926N-linked_GlycosylationPDAPVVTNVTVKARV
CCCCEEEEEEEEEEE		18.82UniProtKB CARBOHYD
935N-linked_GlycosylationTVKARVWNSTFIEDY
EEEEEEECCCCCCCC		28.45UniProtKB CARBOHYD
936PhosphorylationVKARVWNSTFIEDYR
EEEEEECCCCCCCCC		14.69-
937PhosphorylationKARVWNSTFIEDYRD
EEEEECCCCCCCCCC		25.97-
969N-linked_GlycosylationIPTINMENKTTWFSV
CCEECCCCCCEEEEE		35.88UniProtKB CARBOHYD
1016S-palmitoylationIILLLWKCGFFKRAR
HHHHHHHCCHHHHHH		3.7715611341
1024 (in isoform 1)Phosphorylation-21.2226657352
1025 (in isoform 1)Phosphorylation-19.6226657352
1028PhosphorylationRARTRALYEAKRQKA
HHHHHHHHHHHHHHH		16.9228152594
10312-HydroxyisobutyrylationTRALYEAKRQKAEMK
HHHHHHHHHHHHHHH		43.34-
1031UbiquitinationTRALYEAKRQKAEMK
HHHHHHHHHHHHHHH		43.34-
1038UbiquitinationKRQKAEMKSQPSETE
HHHHHHHHCCCCHHH		37.132190698
1038 (in isoform 2)Ubiquitination-37.1321906983
1039PhosphorylationRQKAEMKSQPSETER
HHHHHHHCCCCHHHC		46.1126356563
1042PhosphorylationAEMKSQPSETERLTD
HHHHCCCCHHHCCCC		49.9028355574
1042 (in isoform 1)Phosphorylation-49.9021712546
1044PhosphorylationMKSQPSETERLTDDY
HHCCCCHHHCCCCCC		30.6427794612
1047 (in isoform 1)Phosphorylation-5.1221712546
1048PhosphorylationPSETERLTDDY----
CCHHHCCCCCC----		32.8022617229
1051 (in isoform 1)Phosphorylation-24.2221712546
1051PhosphorylationTERLTDDY-------
HHCCCCCC-------		24.2227273156
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
-KUbiquitinationE3 ubiquitin ligaseN/A#E4P03243#Q6VGT3
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA3_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 ITA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIN1_HUMANBIN1physical
10094488
MSS4_HUMANRABIFphysical
10094488
CD9_HUMANCD9physical
10694273
CD9_HUMANCD9physical
10065872
TSN4_HUMANTSPAN4physical
9360996
EPHA2_HUMANEPHA2physical
23874206
FHL2_HUMANFHL2physical
10906324
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614748Interstitial lung disease, nephrotic syndrome, and epidermolysis bullosa, congenital (ILNEB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1051, AND MASSSPECTROMETRY.

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