ITSN1_MOUSE - dbPTM
ITSN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITSN1_MOUSE
UniProt AC Q9Z0R4
Protein Name Intersectin-1
Gene Name Itsn1
Organism Mus musculus (Mouse).
Sequence Length 1714
Subcellular Localization Endomembrane system. Cell junction, synapse, synaptosome. Cell projection, lamellipodium. Membrane, clathrin-coated pit. Colocalizes with SGIP1 at the plasma membrane in structures corresponding most probably to clathrin-coated pits..
Protein Description Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Inhibits ARHGAP31 activity toward RAC1. Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase..
Protein Sequence MAQFPTPFGGSLDVWAITVEERAKHDQQFLSLKPIAGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSTLPPVMKQQPVAISSAPAFGIGGIASMPPLTAVAPVPMGSIPVVGMSPPLVSSVPPAAVPPLANGAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASAPPAAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGMSVISSSSVDQRLPEEPSSEDEQQPEKKLPVTFEDKKRENFERGSVELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEGTVVLKARRKTLEFELEALNDKKHQLEGKLQDIRCRLATQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILSDQLKQVQQNSLHRDSLLTLKRALEAKELARQQLREQLDEVERETRSKLQEIDVFNNQLKELREIHSKQQLQKQRSLEAARLKQKEQERKSLELEKQKEDAQRRVQERDKQWLEHVQQEEQPRPRKPHEEDRLKREDSVRKKEAEERAKPEMQDKQSRLFHPHQEPAKLATQAPWSTTEKGPLTISAQESVKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENEVPTPAKPVTDLTSAPAPKLALRETPAPLPVTSSEPSTTPNNWADFSSTWPSSSNEKPETDNWDTWAAQPSLTVPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKSDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPVRKSTSIDTGPTESPASLKRVASPAAKPAIPGEEFIAMYTYESSEQGDLTFQQGDVIVVTKKDGDWWTGTVGDKSGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYAATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTSKITPTELPKTAVQPAVCQVIGMYDYTAQNDDELAFSKGQIINVLNKEDPDWWKGEVSGQVGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLTESELLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSCQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
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
122PhosphorylationFGIGGIASMPPLTAV
CCCCCCCCCCCCEEE		29.87-
127PhosphorylationIASMPPLTAVAPVPM
CCCCCCCEEEECCCC		25.51-
182PhosphorylationPAATLPKSSSFSRSG
CCCCCCCCCCCCCCC		27.4326643407
183PhosphorylationAATLPKSSSFSRSGP
CCCCCCCCCCCCCCC		41.3426643407
184PhosphorylationATLPKSSSFSRSGPG
CCCCCCCCCCCCCCC		34.0426643407
186PhosphorylationLPKSSSFSRSGPGSQ
CCCCCCCCCCCCCCH		27.7326643407
188PhosphorylationKSSSFSRSGPGSQLN
CCCCCCCCCCCCHHH		48.4126643407
192PhosphorylationFSRSGPGSQLNTKLQ
CCCCCCCCHHHHHHH		34.3327149854
203PhosphorylationTKLQKAQSFDVASAP
HHHHHHHCCCCCCCC		28.4225521595
208PhosphorylationAQSFDVASAPPAAEW
HHCCCCCCCCCHHHC		40.9525521595
220PhosphorylationAEWAVPQSSRLKYRQ
HHCCCCCHHHHHHHH		16.0320469934
221PhosphorylationEWAVPQSSRLKYRQL
HCCCCCHHHHHHHHH		36.0620469934
313PhosphorylationPSFRRVRSGSGMSVI
CCCCCCCCCCCCEEE		34.1625521595
315PhosphorylationFRRVRSGSGMSVISS
CCCCCCCCCCEEECC		32.3525521595
317OxidationRVRSGSGMSVISSSS
CCCCCCCCEEECCCC		2.8717242355
318PhosphorylationVRSGSGMSVISSSSV
CCCCCCCEEECCCCC		21.5925521595
321PhosphorylationGSGMSVISSSSVDQR
CCCCEEECCCCCCCC		23.2425619855
322PhosphorylationSGMSVISSSSVDQRL
CCCEEECCCCCCCCC		18.6024925903
323PhosphorylationGMSVISSSSVDQRLP
CCEEECCCCCCCCCC		27.8225619855
324PhosphorylationMSVISSSSVDQRLPE
CEEECCCCCCCCCCC		31.4925619855
334PhosphorylationQRLPEEPSSEDEQQP
CCCCCCCCCCCCCCC		50.0325521595
335PhosphorylationRLPEEPSSEDEQQPE
CCCCCCCCCCCCCCC		60.8427087446
361PhosphorylationRENFERGSVELEKRR
HHCCCCCCHHHHHHH		20.7430635358
475UbiquitinationVVLKARRKTLEFELE
EEEEECCCHHHHHHH		52.49-
476PhosphorylationVLKARRKTLEFELEA
EEEECCCHHHHHHHH		29.7025338131
558PhosphorylationLKQVQQNSLHRDSLL
HHHHHHCCCCHHHHH		22.6325521595
563PhosphorylationQNSLHRDSLLTLKRA
HCCCCHHHHHHHHHH		25.8222324799
566PhosphorylationLHRDSLLTLKRALEA
CCHHHHHHHHHHHHH		35.2125338131
574UbiquitinationLKRALEAKELARQQL
HHHHHHHHHHHHHHH		43.83-
607UbiquitinationDVFNNQLKELREIHS
HHHHHHHHHHHHHHC		44.96-
614PhosphorylationKELREIHSKQQLQKQ
HHHHHHHCHHHHHHH		37.5118779572
623PhosphorylationQQLQKQRSLEAARLK
HHHHHHHHHHHHHHH		28.2427087446
638PhosphorylationQKEQERKSLELEKQK
HHHHHHHHHHHHHHH		33.0422324799
685PhosphorylationDRLKREDSVRKKEAE
HHHHHHHHHHHHHHH		21.0429899451
733PhosphorylationEKGPLTISAQESVKV
CCCCEEEECCCEEEE		20.7522324799
737PhosphorylationLTISAQESVKVVYYR
EEEECCCEEEEEEEE		18.3730352176
804PhosphorylationIPENEVPTPAKPVTD
CCCCCCCCCCCCCCC		40.8430352176
814PhosphorylationKPVTDLTSAPAPKLA
CCCCCCCCCCCCCEE		39.28-
837PhosphorylationPVTSSEPSTTPNNWA
CCCCCCCCCCCCCCC		40.6425338131
884PhosphorylationAGQLRQRSAFTPATA
CCCCCCCCCCCCCCC		21.2825619855
887PhosphorylationLRQRSAFTPATATGS
CCCCCCCCCCCCCCC		16.2525619855
890PhosphorylationRSAFTPATATGSSPS
CCCCCCCCCCCCCCC		26.4224925903
892PhosphorylationAFTPATATGSSPSPV
CCCCCCCCCCCCCCC		32.9924925903
894PhosphorylationTPATATGSSPSPVLG
CCCCCCCCCCCCCCC		34.4225521595
895PhosphorylationPATATGSSPSPVLGQ
CCCCCCCCCCCCCCC		30.6425521595
897PhosphorylationTATGSSPSPVLGQGE
CCCCCCCCCCCCCCC		29.5925521595
915PhosphorylationGLQAQALYPWRAKKD
CCCCEECCCCCCCCC		12.0825619855
963PhosphorylationKSYVKLISGPVRKST
HHHEEEECCCCCCCC		47.7029514104
969PhosphorylationISGPVRKSTSIDTGP
ECCCCCCCCCCCCCC		19.4725521595
970PhosphorylationSGPVRKSTSIDTGPT
CCCCCCCCCCCCCCC		32.5124925903
971PhosphorylationGPVRKSTSIDTGPTE
CCCCCCCCCCCCCCC		26.0925521595
974PhosphorylationRKSTSIDTGPTESPA
CCCCCCCCCCCCCCH		43.3125521595
977PhosphorylationTSIDTGPTESPASLK
CCCCCCCCCCCHHHH		50.9024925903
979PhosphorylationIDTGPTESPASLKRV
CCCCCCCCCHHHHHC		28.3925521595
982PhosphorylationGPTESPASLKRVASP
CCCCCCHHHHHCCCC		37.5024925903
984AcetylationTESPASLKRVASPAA
CCCCHHHHHCCCCCC		42.1919860269
988PhosphorylationASLKRVASPAAKPAI
HHHHHCCCCCCCCCC		16.5326824392
1062PhosphorylationGSGTAGKTGSLGKKP
CCCCCCCCCCCCCCH		30.9623984901
1064PhosphorylationGTAGKTGSLGKKPEI
CCCCCCCCCCCCHHH		38.9023984901
1077PhosphorylationEIAQVIASYAATGPE
HHHHHHHHHHCCCHH		12.2723984901
1078PhosphorylationIAQVIASYAATGPEQ
HHHHHHHHHCCCHHH		7.4023984901
1081PhosphorylationVIASYAATGPEQLTL
HHHHHHCCCHHHEEE		45.1323984901
1087PhosphorylationATGPEQLTLAPGQLI
CCCHHHEEECCCEEE		22.1423984901
1125PhosphorylationIGWFPANYVKLLSPG
EEEEEHHHEEEECCC		10.8922499769
1130PhosphorylationANYVKLLSPGTSKIT
HHHEEEECCCCCCCC		31.5525521595
1133PhosphorylationVKLLSPGTSKITPTE
EEEECCCCCCCCCCC		30.1724925903
1134PhosphorylationKLLSPGTSKITPTEL
EEECCCCCCCCCCCC		28.1624925903
1137PhosphorylationSPGTSKITPTELPKT
CCCCCCCCCCCCCCC		28.0925521595
1139PhosphorylationGTSKITPTELPKTAV
CCCCCCCCCCCCCCC		41.3125521595
1199PhosphorylationGQVGLFPSNYVKLTT
CCCEECCCCCEEEEC		33.2028464351
1201PhosphorylationVGLFPSNYVKLTTDM
CEECCCCCEEEECCC		11.8729514104
1201 (in isoform 2)Phosphorylation-11.8729514104
1582PhosphorylationEKAYLVRSQRATGIG
HHHHHHHCCCCCCCC		19.2829899451
1620PhosphorylationYCEVTMGSQCHITKT
CEEEEECCCEEEECC		20.8629899451
1631PhosphorylationITKTIQDTLNPKWNS
EECCHHHHCCCCCCC		16.44-
1638PhosphorylationTLNPKWNSNCQFFIR
HCCCCCCCCCEEEEE		37.5619060867
1663PhosphorylationVFERDQFSPDDFLGR
EEECCCCCCCCCCCC		23.0624925903
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 ITSN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITSN1_MOUSE !!
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 ITSN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_MOUSECblphysical
16914641
SPY2_MOUSESpry2physical
22158968
CBL_HUMANCBLphysical
22158968
CBL_MOUSECblphysical
21712076
DYN1_MOUSEDnm1physical
21712076
EPS15_MOUSEEps15physical
10064583
RHG31_MOUSEArhgap31physical
11744688
CBL_MOUSECblphysical
17875942
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITSN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-318; SER-334;SER-335; SER-895; SER-897 AND THR-977, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1130, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-335 ANDSER-895, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-970, AND MASSSPECTROMETRY.

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