ITSN2_HUMAN - dbPTM
ITSN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITSN2_HUMAN
UniProt AC Q9NZM3
Protein Name Intersectin-2
Gene Name ITSN2
Organism Homo sapiens (Human).
Sequence Length 1697
Subcellular Localization Cytoplasm.
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 (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Plays a role in dendrite formation by melanocytes. [PubMed: 23999003]
Protein Sequence MMAQFPTAMNGGPNMWAITSEERTKHDRQFDNLKPSGGYITGDQARNFFLQSGLPAPVLAEIWALSDLNKDGKMDQQEFSIAMKLIKLKLQGQQLPVVLPPIMKQPPMFSPLISARFGMGSMPNLSIPQPLPPAAPITSLSSATSGTNLPPLMMPTPLVPSVSTSSLPNGTASLIQPLPIPYSSSTLPHGSSYSLMMGGFGGASIQKAQSLIDLGSSSSTSSTASLSGNSPKTGTSEWAVPQPTRLKYRQKFNTLDKSMSGYLSGFQARNALLQSNLSQTQLATIWTLADVDGDGQLKAEEFILAMHLTDMAKAGQPLPLTLPPELVPPSFRGGKQIDSINGTLPSYQKMQEEEPQKKLPVTFEDKRKANYERGNMELEKRRQALMEQQQREAERKAQKEKEEWERKQRELQEQEWKKQLELEKRLEKQRELERQREEERRKDIERREAAKQELERQRRLEWERIRRQELLNQKNREQEEIVRLNSKKKNLHLELEALNGKHQQISGRLQDVRLKKQTQKTELEVLDKQCDLEIMEIKQLQQELQEYQNKLIYLVPEKQLLNERIKNMQFSNTPDSGVSLLHKKSLEKEELCQRLKEQLDALEKETASKLSEMDSFNNQLKCGNMDDSVLQCLLSLLSCLNNLFLLLKELRETYNTQQLALEQLYKIKRDKLKEIERKRLELMQKKKLEDEAARKAKQGKENLWKENLRKEEEEKQKRLQEEKTQEKIQEEERKAEEKQRKDKDTLKAEEKKRETASVLVNYRALYPFEARNHDEMSFNSGDIIQVDEKTVGEPGWLYGSFQGNFGWFPCNYVEKMPSSENEKAVSPKKALLPPTVSLSATSTSSEPLSSNQPASVTDYQNVSFSNLTVNTSWQKKSAFTRTVSPGSVSPIHGQGQVVENLKAQALCSWTAKKDNHLNFSKHDIITVLEQQENWWFGEVHGGRGWFPKSYVKIIPGSEVKREEPEALYAAVNKKPTSAAYSVGEEYIALYPYSSVEPGDLTFTEGEEILVTQKDGEWWTGSIGDRSGIFPSNYVKPKDQESFGSASKSGASNKKPEIAQVTSAYVASGSEQLSLAPGQLILILKKNTSGWWQGELQARGKKRQKGWFPASHVKLLGPSSERATPAFHPVCQVIAMYDYAANNEDELSFSKGQLINVMNKDDPDWWQGEINGVTGLFPSNYVKMTTDSDPSQQWCADLQTLDTMQPIERKRQGYIHELIQTEERYMADLQLVVEVFQKRMAESGFLTEGEMALIFVNWKELIMSNTKLLKALRVRKKTGGEKMPVQMIGDILAAELSHMQAYIRFCSCQLNGAALLQQKTDEDTDFKEFLKKLASDPRCKGMPLSSFLLKPMQRITRYPLLIRSILENTPESHADHSSLKLALERAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLAEQLIFNSLTNCLGPRKLLHSGKLYKTKSNKELHGFLFNDFLLLTYMVKQFAVSSGSEKLFSSKSNAQFKMYKTPIFLNEVLVKLPTDPSSDEPVFHISHIDRVYTLRTDNINERTAWVQKIKAASEQYIDTEKKKREKAYQARSQKTSGIGRLMVHVIEATELKACKPNGKSNPYCEISMGSQSYTTRTIQDTLNPKWNFNCQFFIKDLYQDVLCLTLFDRDQFSPDDFLGRTEIPVAKIRTEQESKGPMTRRLLLHEVPTGEVWVRFDLQLFEQKTLL
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
7Phosphorylation-MMAQFPTAMNGGPN
-CCCCCCCCCCCCCC
39.5720068231
19PhosphorylationGPNMWAITSEERTKH
CCCCEEECHHHHCCC
23.4920068231
20PhosphorylationPNMWAITSEERTKHD
CCCEEECHHHHCCCH
31.2020068231
24PhosphorylationAITSEERTKHDRQFD
EECHHHHCCCHHCCC
35.6920068231
36PhosphorylationQFDNLKPSGGYITGD
CCCCCCCCCCCCCHH
43.1728152594
39PhosphorylationNLKPSGGYITGDQAR
CCCCCCCCCCHHHHH
9.9920090780
41PhosphorylationKPSGGYITGDQARNF
CCCCCCCCHHHHHHH
26.6528152594
89UbiquitinationAMKLIKLKLQGQQLP
HHHHHHHHHCCCCCC
33.49-
110PhosphorylationMKQPPMFSPLISARF
HCCCCCCHHHCHHCC
16.7330266825
114PhosphorylationPMFSPLISARFGMGS
CCCHHHCHHCCCCCC
22.5223403867
126O-linked_GlycosylationMGSMPNLSIPQPLPP
CCCCCCCCCCCCCCC
38.5730059200
138O-linked_GlycosylationLPPAAPITSLSSATS
CCCCCCCCCCCCCCC
23.6630059200
139O-linked_GlycosylationPPAAPITSLSSATSG
CCCCCCCCCCCCCCC
27.2930059200
183O-linked_GlycosylationQPLPIPYSSSTLPHG
CCCCCCCCCCCCCCC
16.6830059200
184O-linked_GlycosylationPLPIPYSSSTLPHGS
CCCCCCCCCCCCCCC
22.8430059200
185O-linked_GlycosylationLPIPYSSSTLPHGSS
CCCCCCCCCCCCCCC
28.2030059200
186O-linked_GlycosylationPIPYSSSTLPHGSSY
CCCCCCCCCCCCCCE
46.3830059200
191O-linked_GlycosylationSSTLPHGSSYSLMMG
CCCCCCCCCEEECCC
24.0630059200
192O-linked_GlycosylationSTLPHGSSYSLMMGG
CCCCCCCCEEECCCC
24.2730059200
193PhosphorylationTLPHGSSYSLMMGGF
CCCCCCCEEECCCCC
13.92-
210PhosphorylationASIQKAQSLIDLGSS
HHHHHHHHHHHCCCC
31.9523401153
216O-linked_GlycosylationQSLIDLGSSSSTSST
HHHHHCCCCCCCCCC
34.0530059200
216PhosphorylationQSLIDLGSSSSTSST
HHHHHCCCCCCCCCC
34.0529255136
217PhosphorylationSLIDLGSSSSTSSTA
HHHHCCCCCCCCCCC
26.8929255136
218PhosphorylationLIDLGSSSSTSSTAS
HHHCCCCCCCCCCCC
39.0629255136
219PhosphorylationIDLGSSSSTSSTASL
HHCCCCCCCCCCCCC
33.9729255136
220O-linked_GlycosylationDLGSSSSTSSTASLS
HCCCCCCCCCCCCCC
28.7530059200
220PhosphorylationDLGSSSSTSSTASLS
HCCCCCCCCCCCCCC
28.7529255136
221PhosphorylationLGSSSSTSSTASLSG
CCCCCCCCCCCCCCC
27.8623403867
222O-linked_GlycosylationGSSSSTSSTASLSGN
CCCCCCCCCCCCCCC
28.2530059200
222PhosphorylationGSSSSTSSTASLSGN
CCCCCCCCCCCCCCC
28.2523403867
223PhosphorylationSSSSTSSTASLSGNS
CCCCCCCCCCCCCCC
21.7423403867
225PhosphorylationSSTSSTASLSGNSPK
CCCCCCCCCCCCCCC
24.1323403867
227PhosphorylationTSSTASLSGNSPKTG
CCCCCCCCCCCCCCC
33.1723403867
230O-linked_GlycosylationTASLSGNSPKTGTSE
CCCCCCCCCCCCCCC
31.1630059200
230PhosphorylationTASLSGNSPKTGTSE
CCCCCCCCCCCCCCC
31.1625159151
233PhosphorylationLSGNSPKTGTSEWAV
CCCCCCCCCCCCCCC
49.42-
244PhosphorylationEWAVPQPTRLKYRQK
CCCCCCCCCCHHHHH
43.30-
248PhosphorylationPQPTRLKYRQKFNTL
CCCCCCHHHHHHHCC
23.91-
254PhosphorylationKYRQKFNTLDKSMSG
HHHHHHHCCCHHHHH
39.1928060719
258PhosphorylationKFNTLDKSMSGYLSG
HHHCCCHHHHHHHHH
20.1824275569
260PhosphorylationNTLDKSMSGYLSGFQ
HCCCHHHHHHHHHHH
31.2319060867
262PhosphorylationLDKSMSGYLSGFQAR
CCHHHHHHHHHHHHH
7.1520090780
278PhosphorylationALLQSNLSQTQLATI
HHHHCCCCHHHHHHE
35.1227251275
280PhosphorylationLQSNLSQTQLATIWT
HHCCCCHHHHHHEEE
23.3627251275
330PhosphorylationPPELVPPSFRGGKQI
CHHHCCCCCCCCCCC
22.8522210691
335AcetylationPPSFRGGKQIDSING
CCCCCCCCCCCCCCC
47.0726051181
339PhosphorylationRGGKQIDSINGTLPS
CCCCCCCCCCCCCCC
21.4122210691
343PhosphorylationQIDSINGTLPSYQKM
CCCCCCCCCCCHHHH
30.89-
346PhosphorylationSINGTLPSYQKMQEE
CCCCCCCCHHHHHCC
43.2230576142
347PhosphorylationINGTLPSYQKMQEEE
CCCCCCCHHHHHCCC
15.3730576142
358UbiquitinationQEEEPQKKLPVTFED
HCCCCCCCCCCCHHH
53.42-
424AcetylationKKQLELEKRLEKQRE
HHHHHHHHHHHHHHH
74.948260223
428AcetylationELEKRLEKQRELERQ
HHHHHHHHHHHHHHH
60.288260235
552PhosphorylationQEYQNKLIYLVPEKQ
HHHHHHHHHHCCHHH
2.3919605366
553PhosphorylationEYQNKLIYLVPEKQL
HHHHHHHHHCCHHHH
16.4525159151
565 (in isoform 4)Ubiquitination-2.8521890473
566UbiquitinationQLLNERIKNMQFSNT
HHHHHHHHCCCCCCC
53.2221890473
571PhosphorylationRIKNMQFSNTPDSGV
HHHCCCCCCCCCCCC
23.9322199227
573PhosphorylationKNMQFSNTPDSGVSL
HCCCCCCCCCCCCHH
27.5525159151
576PhosphorylationQFSNTPDSGVSLLHK
CCCCCCCCCCHHHHH
42.1522199227
579PhosphorylationNTPDSGVSLLHKKSL
CCCCCCCHHHHHHHC
28.8322199227
582 (in isoform 4)Ubiquitination-40.5721890473
583AcetylationSGVSLLHKKSLEKEE
CCCHHHHHHHCCHHH
43.9926051181
583UbiquitinationSGVSLLHKKSLEKEE
CCCHHHHHHHCCHHH
43.9921890473
583 (in isoform 1)Ubiquitination-43.9921890473
583 (in isoform 2)Ubiquitination-43.9921890473
583 (in isoform 3)Ubiquitination-43.9921890473
584UbiquitinationGVSLLHKKSLEKEEL
CCHHHHHHHCCHHHH
49.91-
588AcetylationLHKKSLEKEELCQRL
HHHHHCCHHHHHHHH
62.8826051181
596AcetylationEELCQRLKEQLDALE
HHHHHHHHHHHHHHH
45.6726051181
596UbiquitinationEELCQRLKEQLDALE
HHHHHHHHHHHHHHH
45.67-
613SulfoxidationTASKLSEMDSFNNQL
HHHHHHHHHHHCCCC
4.7421406390
665PhosphorylationQLALEQLYKIKRDKL
HHHHHHHHHHCHHHH
15.4625147952
700UbiquitinationARKAKQGKENLWKEN
HHHHHHHHHHHHHHH
40.72-
705UbiquitinationQGKENLWKENLRKEE
HHHHHHHHHHHHHHH
39.63-
747UbiquitinationRKDKDTLKAEEKKRE
HHCHHHHHHHHHHHH
56.71-
755PhosphorylationAEEKKRETASVLVNY
HHHHHHHHHHHHEEE
28.4122210691
757PhosphorylationEKKRETASVLVNYRA
HHHHHHHHHHEEEEE
24.3322210691
762PhosphorylationTASVLVNYRALYPFE
HHHHHEEEEECCCCC
6.9828509920
766PhosphorylationLVNYRALYPFEARNH
HEEEEECCCCCCCCC
12.6124043423
777PhosphorylationARNHDEMSFNSGDII
CCCCCCCCCCCCCEE
21.1630108239
780PhosphorylationHDEMSFNSGDIIQVD
CCCCCCCCCCEEEEC
35.5130108239
818PhosphorylationNYVEKMPSSENEKAV
CCEEECCCCCCCCCC
46.9526657352
826PhosphorylationSENEKAVSPKKALLP
CCCCCCCCCCCCCCC
35.5427422710
859PhosphorylationQPASVTDYQNVSFSN
CCCCCCCCCCCEEEC
7.8215592455
877PhosphorylationNTSWQKKSAFTRTVS
ECCCEECCCEEEEEC
35.3329514088
880PhosphorylationWQKKSAFTRTVSPGS
CEECCCEEEEECCCC
25.7526074081
882PhosphorylationKKSAFTRTVSPGSVS
ECCCEEEEECCCCCC
23.4429255136
883PhosphorylationKSAFTRTVSPGSVSP
CCCEEEEECCCCCCC
6.1518669648
884PhosphorylationSAFTRTVSPGSVSPI
CCEEEEECCCCCCCC
23.9529255136
886PhosphorylationFTRTVSPGSVSPIHG
EEEEECCCCCCCCCC
32.9218669648
887PhosphorylationTRTVSPGSVSPIHGQ
EEEECCCCCCCCCCC
23.8629255136
888PhosphorylationRTVSPGSVSPIHGQG
EEECCCCCCCCCCCC
11.0618669648
889PhosphorylationTVSPGSVSPIHGQGQ
EECCCCCCCCCCCCH
21.6029255136
908PhosphorylationLKAQALCSWTAKKDN
HHHHHHHHHCCCCCC
28.4525159151
913UbiquitinationLCSWTAKKDNHLNFS
HHHHCCCCCCCCCCC
62.39-
949PhosphorylationGRGWFPKSYVKIIPG
CCCCCCHHHEEEECC
35.0829083192
950PhosphorylationRGWFPKSYVKIIPGS
CCCCCHHHEEEECCC
16.3429083192
952UbiquitinationWFPKSYVKIIPGSEV
CCCHHHEEEECCCHH
27.04-
957PhosphorylationYVKIIPGSEVKREEP
HEEEECCCHHCCCCC
33.5828152594
967PhosphorylationKREEPEALYAAVNKK
CCCCCHHHHHHHHCC
2.5919605366
968PhosphorylationREEPEALYAAVNKKP
CCCCHHHHHHHHCCC
10.2825159151
1041PhosphorylationVKPKDQESFGSASKS
CCCCCHHCCCCCCCC
29.3121815630
1044PhosphorylationKDQESFGSASKSGAS
CCHHCCCCCCCCCCC
27.6221815630
1046PhosphorylationQESFGSASKSGASNK
HHCCCCCCCCCCCCC
29.1121815630
1051PhosphorylationSASKSGASNKKPEIA
CCCCCCCCCCCCCHH
53.3521712546
1118PhosphorylationHVKLLGPSSERATPA
HHEEECCCCCCCCCC
42.9321722762
1119PhosphorylationVKLLGPSSERATPAF
HEEECCCCCCCCCCC
33.9521722762
1123PhosphorylationGPSSERATPAFHPVC
CCCCCCCCCCCCHHH
22.7525159151
1147PhosphorylationANNEDELSFSKGQLI
CCCCCCCCCCCCCEE
25.9824719451
1241 (in isoform 3)Phosphorylation-41.8920068231
1242PhosphorylationFQKRMAESGFLTEGE
HHHHHHHCCCCCCCC
25.8820068231
1242 (in isoform 3)Phosphorylation-25.8820068231
1246PhosphorylationMAESGFLTEGEMALI
HHHCCCCCCCCEEEE
39.4220068231
1249 (in isoform 3)Phosphorylation-18.3020068231
1263PhosphorylationNWKELIMSNTKLLKA
CHHHHHHCCHHHHHH
34.0620068231
1265PhosphorylationKELIMSNTKLLKALR
HHHHHCCHHHHHHHH
18.7620068231
1277PhosphorylationALRVRKKTGGEKMPV
HHHHHHHCCCCCCCH
54.15-
1319PhosphorylationAALLQQKTDEDTDFK
HHHHCCCCCCCCCHH
40.0429759185
1323PhosphorylationQQKTDEDTDFKEFLK
CCCCCCCCCHHHHHH
41.0929396449
1376PhosphorylationPESHADHSSLKLALE
CCCCCCCHHHHHHHH
37.6022210691
1377PhosphorylationESHADHSSLKLALER
CCCCCCHHHHHHHHH
26.5522210691
1479PhosphorylationSGSEKLFSSKSNAQF
CCCHHHHCCCCCCCC
47.4928152594
1480PhosphorylationGSEKLFSSKSNAQFK
CCHHHHCCCCCCCCE
32.5428152594
1482PhosphorylationEKLFSSKSNAQFKMY
HHHHCCCCCCCCEEE
39.0728152594
1523PhosphorylationSHIDRVYTLRTDNIN
EEECEEEEEECCCCC
13.6024719451
1590PhosphorylationACKPNGKSNPYCEIS
ECCCCCCCCCCEEEE
44.4229209046
1593PhosphorylationPNGKSNPYCEISMGS
CCCCCCCCEEEECCC
13.6329209046
1597PhosphorylationSNPYCEISMGSQSYT
CCCCEEEECCCCCEE
8.5229209046
1600PhosphorylationYCEISMGSQSYTTRT
CEEEECCCCCEEECC
13.8125954137
1602PhosphorylationEISMGSQSYTTRTIQ
EEECCCCCEEECCHH
26.5825954137
1603PhosphorylationISMGSQSYTTRTIQD
EECCCCCEEECCHHH
12.4225954137
1604PhosphorylationSMGSQSYTTRTIQDT
ECCCCCEEECCHHHH
18.3029209046
1605PhosphorylationMGSQSYTTRTIQDTL
CCCCCEEECCHHHHC
19.9929209046
1643PhosphorylationLFDRDQFSPDDFLGR
CCCCCCCCCCCCCCC
23.0624076635
1660PhosphorylationIPVAKIRTEQESKGP
CCEEEECCCCCCCCC
45.5623403867
1664PhosphorylationKIRTEQESKGPMTRR
EECCCCCCCCCCCHH
42.4823403867

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 ITSN2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITSN2_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 ITSN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCCIP_HUMANBCCIPphysical
16169070
PTN_HUMANPTNphysical
16169070
TBL3_HUMANTBL3physical
16169070
WASP_HUMANWASphysical
11748279
SEM6A_HUMANSEMA6Aphysical
12421765
YTHD1_HUMANYTHDF1physical
18654987
FNBP4_HUMANFNBP4physical
22558309
SNP29_HUMANSNAP29physical
22558309
NR2C2_HUMANNR2C2physical
22558309
KDM1A_HUMANKDM1Aphysical
22558309
KXDL1_HUMANKXD1physical
22558309
LC7L3_HUMANLUC7L3physical
22558309
EPS15_HUMANEPS15physical
22558309
EP15R_HUMANEPS15L1physical
22558309
RB6I2_HUMANERC1physical
22558309
GOG8A_HUMANGOLGA8Aphysical
22558309
GOGB1_HUMANGOLGB1physical
22558309
HOOK2_HUMANHOOK2physical
22558309
BACD3_HUMANKCTD10physical
22558309
NBR1_HUMANNBR1physical
22558309
MYOME_HUMANPDE4DIPphysical
22558309
BRE1A_HUMANRNF20physical
22558309
STX4_HUMANSTX4physical
22558309
TACC1_HUMANTACC1physical
22558309
TRIO_HUMANTRIOphysical
22558309
ANR17_HUMANANKRD17physical
22558309
DAPLE_HUMANCCDC88Cphysical
22558309
DYST_HUMANDSTphysical
22558309
RABE1_HUMANRABEP1physical
22558309
ROCK1_HUMANROCK1physical
22558309
RUFY1_HUMANRUFY1physical
22558309
TMF1_HUMANTMF1physical
22558309
ANGT_HUMANAGTphysical
22558309
AHDC1_HUMANAHDC1physical
22558309
CBL_HUMANCBLphysical
22558309
CHIC2_HUMANCHIC2physical
22558309
CPSF6_HUMANCPSF6physical
22558309
DYN2_HUMANDNM2physical
22558309
TNFL6_HUMANFASLGphysical
22558309
FCSD1_HUMANFCHSD1physical
22558309
FCSD2_HUMANFCHSD2physical
22558309
GPNMB_HUMANGPNMBphysical
22558309
IP3KA_HUMANITPKAphysical
22558309
LARP6_HUMANLARP6physical
22558309
LTBP4_HUMANLTBP4physical
22558309
MBNL1_HUMANMBNL1physical
22558309
PDC6I_HUMANPDCD6IPphysical
22558309
BCAP_HUMANPIK3AP1physical
22558309
P3C2B_HUMANPIK3C2Bphysical
22558309
RBMX_HUMANRBMXphysical
22558309
REPS1_HUMANREPS1physical
22558309
DLGP1_HUMANDLGAP1physical
22558309
SH3K1_HUMANSH3KBP1physical
22558309
SOS1_HUMANSOS1physical
22558309
SOS2_HUMANSOS2physical
22558309
SYN1_HUMANSYN1physical
22558309
SYNJ2_HUMANSYNJ2physical
22558309
WASL_HUMANWASLphysical
22558309
WASP_HUMANWASphysical
22558309
WIPF1_HUMANWIPF1physical
22558309
WIPF2_HUMANWIPF2physical
22558309
GOGA2_HUMANGOLGA2physical
22558309
SH3G1_HUMANSH3GL1physical
22558309
AMPH_HUMANAMPHphysical
22558309
YLPM1_HUMANYLPM1physical
22558309
WASF2_HUMANWASF2physical
22558309
HNRPK_HUMANHNRNPKphysical
22558309
GARE2_HUMANGAREMLphysical
22558309
ITSN2_HUMANITSN2physical
22558309
KHDR1_HUMANKHDRBS1physical
22745667
EP15R_HUMANEPS15L1physical
20697350
PP1G_HUMANPPP1CCphysical
20697350
EPS15_HUMANEPS15physical
26344197
EP15R_HUMANEPS15L1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITSN2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; TYR-553; THR-882;SER-884; SER-889 AND TYR-968, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884 AND SER-889, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884 AND SER-889, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884 AND SER-889, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, 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-553, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-859 AND TYR-968, ANDMASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-553, AND MASSSPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, AND MASSSPECTROMETRY.

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