ITSN1_HUMAN - dbPTM
ITSN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITSN1_HUMAN
UniProt AC Q15811
Protein Name Intersectin-1
Gene Name ITSN1
Organism Homo sapiens (Human).
Sequence Length 1721
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 Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase (By similarity). 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. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. Inhibits ARHGAP31 activity toward RAC1..
Protein Sequence MAQFPTPFGGSLDIWAITVEERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQLPSALPPVMKQQPVAISSAPAFGMGGIASMPPLTAVAPVPMGSIPVVGMSPTLVSSVPTAAVPPLANGAPPVIQPLPAFAHPAATLPKSSSFSRSGPGSQLNTKLQKAQSFDVASVPPVAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQPLPPVLPPEYIPPSFRRVRSGSGISVISSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQENVKVVYYRALYPFESRSHDEITIQPGDIVMVKGEWVDESQTGEPGWLGGELKGKTGWFPANYAEKIPENEVPAPVKPVTDSTSAPAPKLALRETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLTVPSAGQLRQRSAFTPATATGSSPSPVLGQGEKVEGLQAQALYPWRAKKDNHLNFNKNDVITVLEQQDMWWFGEVQGQKGWFPKSYVKLISGPIRKSTSMDSGSSESPASLKRVASPAAKPVVSGEEFIAMYTYESSEQGDLTFQQGDVILVTKKDGDWWTGTVGDKAGVFPSNYVRLKDSEGSGTAGKTGSLGKKPEIAQVIASYTATGPEQLTLAPGQLILIRKKNPGGWWEGELQARGKKRQIGWFPANYVKLLSPGTSKITPTEPPKSTALAAVCQVIGMYDYTAQNDDELAFNKGQIINVLNKEDPDWWKGEVNGQVGLFPSNYVKLTTDMDPSQQWCSDLHLLDMLTPTERKRQGYIHELIVTEENYVNDLQLVTEIFQKPLMESELLTEKEVAMIFVNWKELIMCNIKLLKALRVRKKMSGEKMPVKMIGDILSAQLPHMQPYIRFCSRQLNGAALIQQKTDEAPDFKEFVKRLAMDPRCKGMPLSSFILKPMQRVTRYPLIIKNILENTPENHPDHSHLKHALEKAEELCSQVNEGVREKENSDRLEWIQAHVQCEGLSEQLVFNSVTNCLGPRKFLHSGKLYKAKSNKELYGFLFNDFLLLTQITKPLGSSGTDKVFSPKSNLQYKMYKTPIFLNEVLVKLPTDPSGDEPIFHISHIDRVYTLRAESINERTAWVQKIKAASELYIETEKKKREKAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTEIRVADIKKDQGSKGPVTKCLLLHEVPTGEIVVRLDLQLFDEP
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
79PhosphorylationRMDQVEFSIAMKLIK
CCCHHHHHHHHHHHH
8.9118767875
182PhosphorylationPAATLPKSSSFSRSG
CCCCCCCCCCCCCCC
29.3126074081
183PhosphorylationAATLPKSSSFSRSGP
CCCCCCCCCCCCCCC
41.3426074081
184PhosphorylationATLPKSSSFSRSGPG
CCCCCCCCCCCCCCC
34.0426074081
186PhosphorylationLPKSSSFSRSGPGSQ
CCCCCCCCCCCCCCH
27.7326074081
188PhosphorylationKSSSFSRSGPGSQLN
CCCCCCCCCCCCHHH
48.4126074081
192PhosphorylationFSRSGPGSQLNTKLQ
CCCCCCCCHHHHHHH
34.3326074081
203PhosphorylationTKLQKAQSFDVASVP
HHHHHCCCCCCCCCC
28.4225159151
208PhosphorylationAQSFDVASVPPVAEW
CCCCCCCCCCCHHHC
34.7025106551
220PhosphorylationAEWAVPQSSRLKYRQ
HHCCCCCHHHHHHHH
16.03-
221PhosphorylationEWAVPQSSRLKYRQL
HCCCCCHHHHHHHHH
36.06-
231PhosphorylationKYRQLFNSHDKTMSG
HHHHHHHCCCCCCCC
26.2328842319
247PhosphorylationLTGPQARTILMQSSL
CCCHHHHHHHHHCCC
22.8322210691
252PhosphorylationARTILMQSSLPQAQL
HHHHHHHCCCCHHHH
21.6322210691
253PhosphorylationRTILMQSSLPQAQLA
HHHHHHCCCCHHHHH
27.4622210691
275PhosphorylationIDQDGKLTAEEFILA
CCCCCCCCHHHHHHH
35.1922468782
291PhosphorylationHLIDVAMSGQPLPPV
HHHHHHHCCCCCCCC
25.2522468782
313PhosphorylationPSFRRVRSGSGISVI
CCCCCCCCCCCEEEE
34.1629255136
315PhosphorylationFRRVRSGSGISVISS
CCCCCCCCCEEEEEC
33.9129255136
318PhosphorylationVRSGSGISVISSTSV
CCCCCCEEEEECCCC
19.5423927012
321PhosphorylationGSGISVISSTSVDQR
CCCEEEEECCCCCCC
25.9624702127
322PhosphorylationSGISVISSTSVDQRL
CCEEEEECCCCCCCC
17.3624702127
323PhosphorylationGISVISSTSVDQRLP
CEEEEECCCCCCCCC
26.4424702127
324PhosphorylationISVISSTSVDQRLPE
EEEEECCCCCCCCCC
26.1623403867
345UbiquitinationEQQQLEKKLPVTFED
HHHHHHHHCCCCCCH
48.96-
353UbiquitinationLPVTFEDKKRENFER
CCCCCCHHHHHHCCC
46.67-
354UbiquitinationPVTFEDKKRENFERG
CCCCCHHHHHHCCCC
76.81-
472AcetylationQEDIVVLKAKKKTLE
HHCEEEEEECCCEEE
46.6920167786
475AcetylationIVVLKAKKKTLEFEL
EEEEEECCCEEEEEH
56.71130715
476UbiquitinationVVLKAKKKTLEFELE
EEEEECCCEEEEEHH
58.60-
477PhosphorylationVLKAKKKTLEFELEA
EEEECCCEEEEEHHH
40.1623403867
495AcetylationKKHQLEGKLQDIRCR
CCHHHHHHHHHHHHH
33.3319608861
545AcetylationLGRLIPEKQILNDQL
HHHHCCHHHHHHHHH
36.9723954790
559PhosphorylationLKQVQQNSLHRDSLV
HHHHHHCCCCHHHHH
22.6321955146
564PhosphorylationQNSLHRDSLVTLKRA
HCCCCHHHHHHHHHH
25.3723403867
567PhosphorylationLHRDSLVTLKRALEA
CCHHHHHHHHHHHHH
31.6729514088
608UbiquitinationDIFNNQLKELREIHN
HHHHHHHHHHHHHHC
44.96-
624PhosphorylationQQLQKQKSMEAERLK
HHHHHHHHHHHHHHH
21.2526657352
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
658 (in isoform 1)Ubiquitination-49.9821890473
658 (in isoform 2)Ubiquitination-49.9821890473
658 (in isoform 3)Ubiquitination-49.9821890473
658 (in isoform 4)Ubiquitination-49.9821890473
658UbiquitinationRRAQERDKQWLEHVQ
HHHHHHHHHHHHHHH
49.9821890473
675UbiquitinationDEHQRPRKLHEEEKL
CCCCCCCHHHHHHHH
57.80-
687PhosphorylationEKLKREESVKKKDGE
HHHHHHHHHHHCCCH
34.1930576142
704UbiquitinationGKQEAQDKLGRLFHQ
HHHHHHHHHHHHHHH
40.54-
717UbiquitinationHQHQEPAKPAVQAPW
HHCCCCCCCCCCCCC
44.20-
729UbiquitinationAPWSTAEKGPLTISA
CCCCCCCCCCEEEEC
64.46-
735PhosphorylationEKGPLTISAQENVKV
CCCCEEEECCCCEEE
20.7525159151
819PhosphorylationPVKPVTDSTSAPAPK
CCCCCCCCCCCCCCC
18.2026074081
820PhosphorylationVKPVTDSTSAPAPKL
CCCCCCCCCCCCCCE
31.5526074081
821PhosphorylationKPVTDSTSAPAPKLA
CCCCCCCCCCCCCEE
35.8926074081
826UbiquitinationSTSAPAPKLALRETP
CCCCCCCCEECCCCC
48.80-
832PhosphorylationPKLALRETPAPLAVT
CCEECCCCCCCEEEE
20.5126074081
839PhosphorylationTPAPLAVTSSEPSTT
CCCCEEEECCCCCCC
22.4129978859
840PhosphorylationPAPLAVTSSEPSTTP
CCCEEEECCCCCCCC
26.5529978859
841PhosphorylationAPLAVTSSEPSTTPN
CCEEEECCCCCCCCC
44.1326074081
844PhosphorylationAVTSSEPSTTPNNWA
EEECCCCCCCCCCCC
40.6426074081
845PhosphorylationVTSSEPSTTPNNWAD
EECCCCCCCCCCCCC
57.9226074081
846PhosphorylationTSSEPSTTPNNWADF
ECCCCCCCCCCCCCC
28.4926074081
854PhosphorylationPNNWADFSSTWPTST
CCCCCCCCCCCCCCC
27.6629978859
855PhosphorylationNNWADFSSTWPTSTN
CCCCCCCCCCCCCCC
34.1929978859
856PhosphorylationNWADFSSTWPTSTNE
CCCCCCCCCCCCCCC
33.9829978859
859PhosphorylationDFSSTWPTSTNEKPE
CCCCCCCCCCCCCCC
39.4829978859
860PhosphorylationFSSTWPTSTNEKPET
CCCCCCCCCCCCCCC
25.7529978859
861PhosphorylationSSTWPTSTNEKPETD
CCCCCCCCCCCCCCC
50.2929978859
891PhosphorylationAGQLRQRSAFTPATA
CCCCCCCCCCCCCCC
21.2826846344
894PhosphorylationLRQRSAFTPATATGS
CCCCCCCCCCCCCCC
16.2526846344
897PhosphorylationRSAFTPATATGSSPS
CCCCCCCCCCCCCCC
26.4226846344
899PhosphorylationAFTPATATGSSPSPV
CCCCCCCCCCCCCCC
32.9926846344
901PhosphorylationTPATATGSSPSPVLG
CCCCCCCCCCCCCCC
34.4229255136
902PhosphorylationPATATGSSPSPVLGQ
CCCCCCCCCCCCCCC
30.6429255136
904PhosphorylationTATGSSPSPVLGQGE
CCCCCCCCCCCCCCC
29.5919664994
922PhosphorylationGLQAQALYPWRAKKD
CCCCEECCCCCCCCC
12.08-
964PhosphorylationQKGWFPKSYVKLISG
CCCCCCHHHEEECCC
35.0829083192
965PhosphorylationKGWFPKSYVKLISGP
CCCCCHHHEEECCCC
14.0229083192
970PhosphorylationKSYVKLISGPIRKST
HHHEEECCCCCCCCC
49.2920068231
976PhosphorylationISGPIRKSTSMDSGS
CCCCCCCCCCCCCCC
18.8325159151
977PhosphorylationSGPIRKSTSMDSGSS
CCCCCCCCCCCCCCC
30.9825159151
978PhosphorylationGPIRKSTSMDSGSSE
CCCCCCCCCCCCCCC
27.9028355574
981PhosphorylationRKSTSMDSGSSESPA
CCCCCCCCCCCCCCH
31.7521712546
983PhosphorylationSTSMDSGSSESPASL
CCCCCCCCCCCCHHH
34.5829255136
984PhosphorylationTSMDSGSSESPASLK
CCCCCCCCCCCHHHH
45.6929255136
986PhosphorylationMDSGSSESPASLKRV
CCCCCCCCCHHHHHH
27.9329255136
989PhosphorylationGSSESPASLKRVASP
CCCCCCHHHHHHCCC
37.5029255136
995PhosphorylationASLKRVASPAAKPVV
HHHHHHCCCCCCCCC
16.5326657352
1040PhosphorylationKKDGDWWTGTVGDKA
ECCCCEEEEEECCCC
20.7926091039
1042PhosphorylationDGDWWTGTVGDKAGV
CCCEEEEEECCCCCC
17.5926091039
1052PhosphorylationDKAGVFPSNYVRLKD
CCCCCCCCCCEEEEC
29.3626091039
1054PhosphorylationAGVFPSNYVRLKDSE
CCCCCCCCEEEECCC
7.4123822953
1069PhosphorylationGSGTAGKTGSLGKKP
CCCCCCCCCCCCCCH
30.9622210691
1071PhosphorylationGTAGKTGSLGKKPEI
CCCCCCCCCCCCHHH
38.9028464451
1084PhosphorylationEIAQVIASYTATGPE
HHHHHHHHHCCCCHH
16.3428857561
1088PhosphorylationVIASYTATGPEQLTL
HHHHHCCCCHHHEEE
45.5328464451
1132PhosphorylationIGWFPANYVKLLSPG
EEEEEHHHEEEECCC
10.8923822953
1137PhosphorylationANYVKLLSPGTSKIT
HHHEEEECCCCCCCC
31.5528555341
1140PhosphorylationVKLLSPGTSKITPTE
EEEECCCCCCCCCCC
30.1723403867
1141PhosphorylationKLLSPGTSKITPTEP
EEECCCCCCCCCCCC
28.1623403867
1144PhosphorylationSPGTSKITPTEPPKS
CCCCCCCCCCCCCHH
28.0925159151
1146PhosphorylationGTSKITPTEPPKSTA
CCCCCCCCCCCHHHH
53.1023403867
1206PhosphorylationGQVGLFPSNYVKLTT
CEEEECCCCCEEEEC
33.2025627689
1208PhosphorylationVGLFPSNYVKLTTDM
EEECCCCCEEEECCC
11.8725159151
1303UbiquitinationLKALRVRKKMSGEKM
HHHHHHHHHCCCCCC
50.39-
1383PhosphorylationLKPMQRVTRYPLIIK
CHHHHHHCCHHHHHH
27.03-
1466PhosphorylationGPRKFLHSGKLYKAK
CHHHHHHCCCEEECC
39.5126437602
1501PhosphorylationKPLGSSGTDKVFSPK
CCCCCCCCCCCCCCC
34.30-
1506PhosphorylationSGTDKVFSPKSNLQY
CCCCCCCCCCCCCCE
34.1124719451
1550PhosphorylationSHIDRVYTLRAESIN
EEECEEEEEECHHHC
13.6024719451
1560PhosphorylationAESINERTAWVQKIK
CHHHCHHHHHHHHHH
20.7720068231
1645PhosphorylationTLNPKWNSNCQFFIR
HCCCCCCCCCEEEEE
37.56-
1670PhosphorylationVFERDQFSPDDFLGR
EEECCCCCCCCCCCC
23.0624076635

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 ligaseITCHQ96J02
PMID:29851086

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITSN1_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 ITSN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMRC2_HUMANSMARCC2physical
16169070
RM20_HUMANMRPL20physical
16169070
SNX5_HUMANSNX5physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
KIF5A_HUMANKIF5Aphysical
16169070
U119A_HUMANUNC119physical
16169070
SNP25_HUMANSNAP25physical
10373452
SNP23_HUMANSNAP23physical
10373452
EPHB2_HUMANEPHB2physical
12389031
CDC42_HUMANCDC42physical
11584276
WASL_HUMANWASLphysical
11584276
CDC42_HUMANCDC42physical
12006984
AP2B1_HUMANAP2B1physical
18654987
ASAP2_HUMANASAP2physical
18654987
CBL_HUMANCBLphysical
18654987
BCAP_HUMANPIK3AP1physical
18654987
PFD5_HUMANPFDN5physical
18654987
SF3B4_HUMANSF3B4physical
18654987
CCNO_HUMANCCNOphysical
18654987
WBP11_HUMANWBP11physical
18654987
EPN2_HUMANEPN2physical
22558309
PICAL_HUMANPICALMphysical
22558309
FNBP4_HUMANFNBP4physical
22558309
FOG2_HUMANZFPM2physical
22558309
AGFG1_HUMANAGFG1physical
22558309
RFIP2_HUMANRAB11FIP2physical
22558309
DAB2_HUMANDAB2physical
22558309
AGFG2_HUMANAGFG2physical
22558309
CLIP2_HUMANCLIP2physical
22558309
EP15R_HUMANEPS15L1physical
22558309
GOGA5_HUMANGOLGA5physical
22558309
ITSN1_HUMANITSN1physical
22558309
PEPL_HUMANPPLphysical
22558309
P85A_HUMANPIK3R1physical
22558309
LIPA2_HUMANPPFIA2physical
22558309
CYH1_HUMANCYTH1physical
22558309
BRE1B_HUMANRNF40physical
22558309
SPDLY_HUMANSPDL1physical
22558309
CLH1_HUMANCLTCphysical
22558309
EPS15_HUMANEPS15physical
22558309
KI16B_HUMANKIF16Bphysical
22558309
ARFP2_HUMANARFIP2physical
22558309
DESM_HUMANDESphysical
22558309
FNBP1_HUMANFNBP1physical
22558309
GCC1_HUMANGCC1physical
22558309
HIP1_HUMANHIP1physical
22558309
MTUS2_HUMANMTUS2physical
22558309
CE85L_HUMANCEP85Lphysical
22558309
PACN3_HUMANPACSIN3physical
22558309
PDC6I_HUMANPDCD6IPphysical
22558309
PREX1_HUMANPREX1physical
22558309
RABE1_HUMANRABEP1physical
22558309
RAI14_HUMANRAI14physical
22558309
SCOC_HUMANSCOCphysical
22558309
TRIM8_HUMANTRIM8physical
22558309
P3C2B_HUMANPIK3C2Bphysical
22558309
GARE2_HUMANGAREMLphysical
22558309
SPY2_HUMANSPRY2physical
22558309
DLGP1_HUMANDLGAP1physical
22558309
SYNJ2_HUMANSYNJ2physical
22558309
AP2B1_HUMANAP2B1physical
22558309
FCSD2_HUMANFCHSD2physical
22558309
PICAL_MOUSEPicalmphysical
22558309
EPN2_MOUSEEpn2physical
22558309
AGFG2_MOUSEAgfg2physical
22558309
AGFG1_MOUSEAgfg1physical
22558309
EP15R_MOUSEEps15l1physical
22558309
AMOL1_MOUSEAmotl1physical
22558309
BECN1_MOUSEBecn1physical
22558309
HM20A_MOUSEHmg20aphysical
22558309
K2C1_MOUSEKrt1physical
22558309
K2C71_MOUSEKrt71physical
22558309
K2C79_MOUSEKrt79physical
22558309
PEPL_MOUSEPplphysical
22558309
SWP70_MOUSESwap70physical
22558309
SYNCI_MOUSESyncphysical
22558309
DLGP2_MOUSEDlgap2physical
22558309
PLVAP_MOUSEPlvapphysical
22558309
SPY2_MOUSESpry2physical
22558309
P53_MOUSETrp53physical
22558309
ITSN2_HUMANITSN2physical
22558309
RAB5A_HUMANRAB5Aphysical
22558309
ARF6_HUMANARF6physical
22558309
PDE4D_HUMANPDE4Dphysical
22558309
DISC1_HUMANDISC1physical
22558309
SH3K1_HUMANSH3KBP1physical
19166927
ITSN1_HUMANITSN1physical
21712076
CBL_HUMANCBLphysical
21712076
REPS1_HUMANREPS1physical
20946875
SYNJ1_HUMANSYNJ1physical
18539136
WASP_HUMANWASphysical
18539136
SOS1_HUMANSOS1physical
18539136
CBL_HUMANCBLphysical
18539136
CBLB_HUMANCBLBphysical
18539136
EPS15_HUMANEPS15physical
10064583
SOS1_HUMANSOS1physical
15824104
WASP_HUMANWASphysical
15824104
TTC37_HUMANTTC37physical
22939629
SKIV2_HUMANSKIV2Lphysical
22939629
SETD3_HUMANSETD3physical
22939629
RNH2A_HUMANRNASEH2Aphysical
22939629
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 ITSN1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-495, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-315; SER-902; SER-904;SER-978 AND SER-986, AND MASS 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-902 AND SER-904, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904, AND MASSSPECTROMETRY.

TOP