VCIP1_HUMAN - dbPTM
VCIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VCIP1_HUMAN
UniProt AC Q96JH7
Protein Name Deubiquitinating protein VCIP135
Gene Name VCPIP1
Organism Homo sapiens (Human).
Sequence Length 1222
Subcellular Localization Endoplasmic reticulum. Golgi apparatus, Golgi stack. Associated with Golgi stacks and endoplasmic reticulum..
Protein Description Acts as a deubiquitinating enzyme. Necessary for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Mediates dissociation of the ternary complex containing STX5A, NSFL1C and VCP (By similarity). Hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains..
Protein Sequence MSQPPPPPPPLPPPPPPPEAPQTPSSLASAAASGGLLKRRDRRILSGSCPDPKCQARLFFPASGSVSIECTECGQRHEQQQLLGVEEVTDPDVVLHNLLRNALLGVTGAPKKNTELVKVMGLSNYHCKLLSPILARYGMDKQTGRAKLLRDMNQGELFDCALLGDRAFLIEPEHVNTVGYGKDRSGSLLYLHDTLEDIKRANKSQECLIPVHVDGDGHCLVHAVSRALVGRELFWHALRENLKQHFQQHLARYQALFHDFIDAAEWEDIINECDPLFVPPEGVPLGLRNIHIFGLANVLHRPIILLDSLSGMRSSGDYSATFLPGLIPAEKCTGKDGHLNKPICIAWSSSGRNHYIPLVGIKGAALPKLPMNLLPKAWGVPQDLIKKYIKLEEDGGCVIGGDRSLQDKYLLRLVAAMEEVFMDKHGIHPSLVADVHQYFYRRTGVIGVQPEEVTAAAKKAVMDNRLHKCLLCGALSELHVPPEWLAPGGKLYNLAKSTHGQLRTDKNYSFPLNNLVCSYDSVKDVLVPDYGMSNLTACNWCHGTSVRKVRGDGSIVYLDGDRTNSRSTGGKCGCGFKHFWDGKEYDNLPEAFPITLEWGGRVVRETVYWFQYESDSSLNSNVYDVAMKLVTKHFPGEFGSEILVQKVVHTILHQTAKKNPDDYTPVNIDGAHAQRVGDVQGQESESQLPTKIILTGQKTKTLHKEELNMSKTERTIQQNITEQASVMQKRKTEKLKQEQKGQPRTVSPSTIRDGPSSAPATPTKAPYSPTTSKEKKIRITTNDGRQSMVTLKSSTTFFELQESIAREFNIPPYLQCIRYGFPPKELMPPQAGMEKEPVPLQHGDRITIEILKSKAEGGQSAAAHSAHTVKQEDIAVTGKLSSKELQEQAEKEMYSLCLLATLMGEDVWSYAKGLPHMFQQGGVFYSIMKKTMGMADGKHCTFPHLPGKTFVYNASEDRLELCVDAAGHFPIGPDVEDLVKEAVSQVRAEATTRSRESSPSHGLLKLGSGGVVKKKSEQLHNVTAFQGKGHSLGTASGNPHLDPRARETSVVRKHNTGTDFSNSSTKTEPSVFTASSSNSELIRIAPGVVTMRDGRQLDPDLVEAQRKKLQEMVSSIQASMDRHLRDQSTEQSPSDLPQRKTEVVSSSAKSGSLQTGLPESFPLTGGTENLNTETTDGCVADALGAAFATRSKAQRGNSVEELEEMDSQDAEMTNTTEPMDHS
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
2Phosphorylation------MSQPPPPPP
------CCCCCCCCC
63.8028348404
23PhosphorylationPPPEAPQTPSSLASA
CCCCCCCCCCHHHHH
24.8724719451
25PhosphorylationPEAPQTPSSLASAAA
CCCCCCCCHHHHHHH
41.1828348404
26PhosphorylationEAPQTPSSLASAAAS
CCCCCCCHHHHHHHH
29.2028348404
46PhosphorylationRRDRRILSGSCPDPK
HHCCCCCCCCCCCCC
26.7029978859
48PhosphorylationDRRILSGSCPDPKCQ
CCCCCCCCCCCCCCC
21.0729978859
53UbiquitinationSGSCPDPKCQARLFF
CCCCCCCCCCEEEEE
46.4924816145
65PhosphorylationLFFPASGSVSIECTE
EEEECCCEEEEEEEC
15.3627251275
67PhosphorylationFPASGSVSIECTECG
EECCCEEEEEEECCC
17.8627251275
111UbiquitinationLGVTGAPKKNTELVK
HCCCCCCCCCCHHHH
59.1129967540
112UbiquitinationGVTGAPKKNTELVKV
CCCCCCCCCCHHHHH
68.9623503661
114PhosphorylationTGAPKKNTELVKVMG
CCCCCCCCHHHHHHC
39.3129759185
118UbiquitinationKKNTELVKVMGLSNY
CCCCHHHHHHCCCCH
38.8423503661
125PhosphorylationKVMGLSNYHCKLLSP
HHHCCCCHHHHHHHH
12.7629759185
128UbiquitinationGLSNYHCKLLSPILA
CCCCHHHHHHHHHHH
38.8729967540
131PhosphorylationNYHCKLLSPILARYG
CHHHHHHHHHHHHHC
21.9628450419
137PhosphorylationLSPILARYGMDKQTG
HHHHHHHHCCCCCCC
15.9320068231
141UbiquitinationLARYGMDKQTGRAKL
HHHHCCCCCCCHHHH
40.6529967540
182UbiquitinationVNTVGYGKDRSGSLL
CCCCCCCCCCCCCEE
41.2921906983
185PhosphorylationVGYGKDRSGSLLYLH
CCCCCCCCCCEEEEE
42.7530108239
187PhosphorylationYGKDRSGSLLYLHDT
CCCCCCCCEEEEECC
19.2230108239
190PhosphorylationDRSGSLLYLHDTLED
CCCCCEEEEECCHHH
13.7923312004
194PhosphorylationSLLYLHDTLEDIKRA
CEEEEECCHHHHHHH
22.6923312004
199UbiquitinationHDTLEDIKRANKSQE
ECCHHHHHHHCCCCC
58.7530230243
203UbiquitinationEDIKRANKSQECLIP
HHHHHHCCCCCCEEE
53.1630230243
243AcetylationHALRENLKQHFQQHL
HHHHHHHHHHHHHHH
53.9919828469
314PhosphorylationDSLSGMRSSGDYSAT
HCCCCCCCCCCCCCC
29.7628857561
315PhosphorylationSLSGMRSSGDYSATF
CCCCCCCCCCCCCCC
25.8928857561
318PhosphorylationGMRSSGDYSATFLPG
CCCCCCCCCCCCCCC
12.0628857561
319PhosphorylationMRSSGDYSATFLPGL
CCCCCCCCCCCCCCC
26.1027080861
321PhosphorylationSSGDYSATFLPGLIP
CCCCCCCCCCCCCCC
21.5527080861
331UbiquitinationPGLIPAEKCTGKDGH
CCCCCHHHCCCCCCC
38.9221963094
335UbiquitinationPAEKCTGKDGHLNKP
CHHHCCCCCCCCCCC
42.2422817900
341UbiquitinationGKDGHLNKPICIAWS
CCCCCCCCCEEEEEC
41.9629967540
355PhosphorylationSSSGRNHYIPLVGIK
CCCCCCCEEEEEEEC
14.0527642862
362UbiquitinationYIPLVGIKGAALPKL
EEEEEEECCCCCCCC
36.2522505724
368UbiquitinationIKGAALPKLPMNLLP
ECCCCCCCCCCCCCH
67.1030230243
376UbiquitinationLPMNLLPKAWGVPQD
CCCCCCHHHHCCCHH
57.6622817900
386UbiquitinationGVPQDLIKKYIKLEE
CCCHHHHHHHCCEEC
46.9822505724
387UbiquitinationVPQDLIKKYIKLEED
CCHHHHHHHCCEECC
45.2623503661
390AcetylationDLIKKYIKLEEDGGC
HHHHHHCCEECCCCE
46.917706123
390UbiquitinationDLIKKYIKLEEDGGC
HHHHHHCCEECCCCE
46.9123503661
408AcetylationGDRSLQDKYLLRLVA
CCCHHCHHHHHHHHH
25.4919608861
408UbiquitinationGDRSLQDKYLLRLVA
CCCHHCHHHHHHHHH
25.4919608861
408MalonylationGDRSLQDKYLLRLVA
CCCHHCHHHHHHHHH
25.4926320211
409PhosphorylationDRSLQDKYLLRLVAA
CCHHCHHHHHHHHHH
21.18-
458UbiquitinationEEVTAAAKKAVMDNR
HHHHHHHHHHHHCCH
36.2221906983
459UbiquitinationEVTAAAKKAVMDNRL
HHHHHHHHHHHCCHH
41.3022817900
496UbiquitinationGKLYNLAKSTHGQLR
CHHHHHHHHCCCCCC
60.0830230243
506UbiquitinationHGQLRTDKNYSFPLN
CCCCCCCCCCCCCCC
58.1129967540
509PhosphorylationLRTDKNYSFPLNNLV
CCCCCCCCCCCCCEE
29.7630387612
518PhosphorylationPLNNLVCSYDSVKDV
CCCCEEECCCHHHCE
25.2130387612
521PhosphorylationNLVCSYDSVKDVLVP
CEEECCCHHHCEECC
23.8830387612
533PhosphorylationLVPDYGMSNLTACNW
ECCCCCCCCCCCCCC
25.0727251275
536PhosphorylationDYGMSNLTACNWCHG
CCCCCCCCCCCCCCC
33.1527251275
544PhosphorylationACNWCHGTSVRKVRG
CCCCCCCCCEEEEEC
10.6127251275
545PhosphorylationCNWCHGTSVRKVRGD
CCCCCCCCEEEEECC
25.2327080861
554PhosphorylationRKVRGDGSIVYLDGD
EEEECCCCEEEEECC
17.3928857561
557PhosphorylationRGDGSIVYLDGDRTN
ECCCCEEEEECCCCC
9.4528796482
563PhosphorylationVYLDGDRTNSRSTGG
EEEECCCCCCCCCCC
42.1423403867
571UbiquitinationNSRSTGGKCGCGFKH
CCCCCCCCCCCCCCC
28.8829967540
632UbiquitinationVAMKLVTKHFPGEFG
HHHHHHHHHCCCCCC
35.4529967540
646UbiquitinationGSEILVQKVVHTILH
CHHHHHHHHHHHHHH
38.4529967540
657UbiquitinationTILHQTAKKNPDDYT
HHHHHHHHHCCCCCC
57.3729967540
658UbiquitinationILHQTAKKNPDDYTP
HHHHHHHHCCCCCCC
71.8530230243
663PhosphorylationAKKNPDDYTPVNIDG
HHHCCCCCCCCCCCC
21.9628796482
664PhosphorylationKKNPDDYTPVNIDGA
HHCCCCCCCCCCCCC
27.9628796482
691UbiquitinationSESQLPTKIILTGQK
CCCCCCCEEEECCCC
26.3021906983
695PhosphorylationLPTKIILTGQKTKTL
CCCEEEECCCCCCCC
27.4528555341
698UbiquitinationKIILTGQKTKTLHKE
EEEECCCCCCCCCHH
54.0227667366
698AcetylationKIILTGQKTKTLHKE
EEEECCCCCCCCCHH
54.0225953088
700UbiquitinationILTGQKTKTLHKEEL
EECCCCCCCCCHHHH
57.00-
704UbiquitinationQKTKTLHKEELNMSK
CCCCCCCHHHHCCCH
56.8729967540
710PhosphorylationHKEELNMSKTERTIQ
CHHHHCCCHHHHHHH
35.0429214152
725PhosphorylationQNITEQASVMQKRKT
HHHHHHHHHHHHHHH
20.1628857561
729UbiquitinationEQASVMQKRKTEKLK
HHHHHHHHHHHHHHH
37.4523000965
731UbiquitinationASVMQKRKTEKLKQE
HHHHHHHHHHHHHHH
68.9823000965
732PhosphorylationSVMQKRKTEKLKQEQ
HHHHHHHHHHHHHHH
42.24-
734UbiquitinationMQKRKTEKLKQEQKG
HHHHHHHHHHHHHCC
67.2423000965
736UbiquitinationKRKTEKLKQEQKGQP
HHHHHHHHHHHCCCC
63.9624816145
745PhosphorylationEQKGQPRTVSPSTIR
HHCCCCCCCCCCCCC
31.8322115753
747PhosphorylationKGQPRTVSPSTIRDG
CCCCCCCCCCCCCCC
16.7225159151
749PhosphorylationQPRTVSPSTIRDGPS
CCCCCCCCCCCCCCC
29.0325159151
750PhosphorylationPRTVSPSTIRDGPSS
CCCCCCCCCCCCCCC
24.3425159151
756PhosphorylationSTIRDGPSSAPATPT
CCCCCCCCCCCCCCC
44.6630266825
757PhosphorylationTIRDGPSSAPATPTK
CCCCCCCCCCCCCCC
41.2129255136
761PhosphorylationGPSSAPATPTKAPYS
CCCCCCCCCCCCCCC
30.3629255136
763PhosphorylationSSAPATPTKAPYSPT
CCCCCCCCCCCCCCC
35.1727273156
764UbiquitinationSAPATPTKAPYSPTT
CCCCCCCCCCCCCCC
48.8727667366
767PhosphorylationATPTKAPYSPTTSKE
CCCCCCCCCCCCCCC
31.9430266825
768PhosphorylationTPTKAPYSPTTSKEK
CCCCCCCCCCCCCCC
18.0825159151
770PhosphorylationTKAPYSPTTSKEKKI
CCCCCCCCCCCCCEE
37.4530266825
771PhosphorylationKAPYSPTTSKEKKIR
CCCCCCCCCCCCEEE
40.9830266825
772PhosphorylationAPYSPTTSKEKKIRI
CCCCCCCCCCCEEEE
41.1030266825
773UbiquitinationPYSPTTSKEKKIRIT
CCCCCCCCCCEEEEE
72.0327667366
780PhosphorylationKEKKIRITTNDGRQS
CCCEEEEECCCCCEE
15.0826074081
781PhosphorylationEKKIRITTNDGRQSM
CCEEEEECCCCCEEE
29.0126074081
852UbiquitinationRITIEILKSKAEGGQ
EEEEEEEHHHCCCCC
56.4233845483
854UbiquitinationTIEILKSKAEGGQSA
EEEEEHHHCCCCCCC
49.2029967540
860PhosphorylationSKAEGGQSAAAHSAH
HHCCCCCCCCHHCCC
24.1329900121
865PhosphorylationGQSAAAHSAHTVKQE
CCCCCHHCCCCCCHH
19.6129900121
868PhosphorylationAAAHSAHTVKQEDIA
CCHHCCCCCCHHHHH
29.1629900121
870UbiquitinationAHSAHTVKQEDIAVT
HHCCCCCCHHHHHHH
49.4722817900
877PhosphorylationKQEDIAVTGKLSSKE
CHHHHHHHCCCCHHH
21.4129900121
879UbiquitinationEDIAVTGKLSSKELQ
HHHHHHCCCCHHHHH
35.5127667366
881PhosphorylationIAVTGKLSSKELQEQ
HHHHCCCCHHHHHHH
42.7327251275
883UbiquitinationVTGKLSSKELQEQAE
HHCCCCHHHHHHHHH
60.1021906983
929UbiquitinationGVFYSIMKKTMGMAD
CHHHHHHHHHHCCCC
43.3423503661
930UbiquitinationVFYSIMKKTMGMADG
HHHHHHHHHHCCCCC
26.7723503661
938UbiquitinationTMGMADGKHCTFPHL
HHCCCCCCCCCCCCC
35.7329967540
948UbiquitinationTFPHLPGKTFVYNAS
CCCCCCCCEEEEECC
36.5329967540
991PhosphorylationSQVRAEATTRSRESS
HHHHHHHHCCCCCCC
17.7823401153
992PhosphorylationQVRAEATTRSRESSP
HHHHHHHCCCCCCCC
33.4223403867
994PhosphorylationRAEATTRSRESSPSH
HHHHHCCCCCCCCCC
38.0022167270
997PhosphorylationATTRSRESSPSHGLL
HHCCCCCCCCCCCCE
46.5722167270
997O-linked_GlycosylationATTRSRESSPSHGLL
HHCCCCCCCCCCCCE
46.5728657654
998PhosphorylationTTRSRESSPSHGLLK
HCCCCCCCCCCCCEE
26.1822167270
1000PhosphorylationRSRESSPSHGLLKLG
CCCCCCCCCCCEECC
31.9430266825
1005UbiquitinationSPSHGLLKLGSGGVV
CCCCCCEECCCCCEE
56.7133845483
1008PhosphorylationHGLLKLGSGGVVKKK
CCCEECCCCCEEECC
42.6925159151
1013UbiquitinationLGSGGVVKKKSEQLH
CCCCCEEECCHHHHC
52.6733845483
1014UbiquitinationGSGGVVKKKSEQLHN
CCCCEEECCHHHHCC
50.3429967540
1015UbiquitinationSGGVVKKKSEQLHNV
CCCEEECCHHHHCCE
54.2133845483
1016PhosphorylationGGVVKKKSEQLHNVT
CCEEECCHHHHCCEE
39.1826074081
1028UbiquitinationNVTAFQGKGHSLGTA
CEEEECCCCCCCCCC
42.5423000965
1031PhosphorylationAFQGKGHSLGTASGN
EECCCCCCCCCCCCC
36.8428555341
1053UbiquitinationRETSVVRKHNTGTDF
CCCCCEEECCCCCCC
29.6023000965
1056PhosphorylationSVVRKHNTGTDFSNS
CCEEECCCCCCCCCC
40.9727251275
1058PhosphorylationVRKHNTGTDFSNSST
EEECCCCCCCCCCCC
31.6527251275
1061PhosphorylationHNTGTDFSNSSTKTE
CCCCCCCCCCCCCCC
38.3228348404
1063PhosphorylationTGTDFSNSSTKTEPS
CCCCCCCCCCCCCCC
37.8825849741
1064PhosphorylationGTDFSNSSTKTEPSV
CCCCCCCCCCCCCCE
37.8728348404
1065PhosphorylationTDFSNSSTKTEPSVF
CCCCCCCCCCCCCEE
41.6328348404
1066UbiquitinationDFSNSSTKTEPSVFT
CCCCCCCCCCCCEEE
53.4929967540
1067PhosphorylationFSNSSTKTEPSVFTA
CCCCCCCCCCCEEEC
53.9028348404
1070PhosphorylationSSTKTEPSVFTASSS
CCCCCCCCEEECCCC
24.5128555341
1073PhosphorylationKTEPSVFTASSSNSE
CCCCCEEECCCCCCC
24.3923186163
1075PhosphorylationEPSVFTASSSNSELI
CCCEEECCCCCCCEE
31.1023186163
1076PhosphorylationPSVFTASSSNSELIR
CCEEECCCCCCCEEE
30.9528857561
1076O-linked_GlycosylationPSVFTASSSNSELIR
CCEEECCCCCCCEEE
30.9528657654
1077PhosphorylationSVFTASSSNSELIRI
CEEECCCCCCCEEEE
41.7128857561
1079O-linked_GlycosylationFTASSSNSELIRIAP
EECCCCCCCEEEECC
35.4128657654
1079PhosphorylationFTASSSNSELIRIAP
EECCCCCCCEEEECC
35.4128857561
1091SulfoxidationIAPGVVTMRDGRQLD
ECCCEEECCCCCCCC
2.1921406390
1108MethylationLVEAQRKKLQEMVSS
HHHHHHHHHHHHHHH
58.55-
1108UbiquitinationLVEAQRKKLQEMVSS
HHHHHHHHHHHHHHH
58.5529967540
1115PhosphorylationKLQEMVSSIQASMDR
HHHHHHHHHHHHHHH
13.8128348404
1119PhosphorylationMVSSIQASMDRHLRD
HHHHHHHHHHHHHHC
12.5824719451
1125MethylationASMDRHLRDQSTEQS
HHHHHHHHCCCCCCC
33.52115919773
1128PhosphorylationDRHLRDQSTEQSPSD
HHHHHCCCCCCCCCC
37.9026055452
1129PhosphorylationRHLRDQSTEQSPSDL
HHHHCCCCCCCCCCC
32.2020068231
1132PhosphorylationRDQSTEQSPSDLPQR
HCCCCCCCCCCCCCC
21.8225159151
1134PhosphorylationQSTEQSPSDLPQRKT
CCCCCCCCCCCCCCH
57.9628985074
1140UbiquitinationPSDLPQRKTEVVSSS
CCCCCCCCHHHCCCC
43.7329967540
1141PhosphorylationSDLPQRKTEVVSSSA
CCCCCCCHHHCCCCC
35.8829978859
1145PhosphorylationQRKTEVVSSSAKSGS
CCCHHHCCCCCCCCC
24.6129978859
1146PhosphorylationRKTEVVSSSAKSGSL
CCHHHCCCCCCCCCC
23.7829978859
1147PhosphorylationKTEVVSSSAKSGSLQ
CHHHCCCCCCCCCCC
32.0129978859
1174PhosphorylationTENLNTETTDGCVAD
CCCCCCCCCCCHHHH
28.3126074081
1175PhosphorylationENLNTETTDGCVADA
CCCCCCCCCCHHHHH
24.9426074081
1189PhosphorylationALGAAFATRSKAQRG
HHHHHHHHHHHHHCC
29.0826074081
1191PhosphorylationGAAFATRSKAQRGNS
HHHHHHHHHHHCCCC
28.1726074081
1198PhosphorylationSKAQRGNSVEELEEM
HHHHCCCCHHHHHHH
33.4630278072
1207PhosphorylationEELEEMDSQDAEMTN
HHHHHHHHHCHHHCC
28.7523927012
1213PhosphorylationDSQDAEMTNTTEPMD
HHHCHHHCCCCCCCC
22.4022199227
1215PhosphorylationQDAEMTNTTEPMDHS
HCHHHCCCCCCCCCC
24.3022199227
1216PhosphorylationDAEMTNTTEPMDHS-
CHHHCCCCCCCCCC-
39.9122199227
1222PhosphorylationTTEPMDHS-------
CCCCCCCC-------
37.3422199227

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
761TPhosphorylationKinaseCDK1P06493
PSP
768SPhosphorylationKinaseCDK1P06493
PSP
1207SPhosphorylationKinaseATMQ13315
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1207SPhosphorylation

32649882

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 VCIP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFD1_HUMANUFD1Lphysical
19615732
TERA_HUMANVCPphysical
19615732
HUWE1_HUMANHUWE1physical
19615732
FAF2_HUMANFAF2physical
19615732
NPL4_HUMANNPLOC4physical
19615732
NSF1C_HUMANNSFL1Cphysical
19615732
MRP9_HUMANABCC12physical
19615732
UBX2B_HUMANUBXN2Bphysical
19615732
UBX2A_HUMANUBXN2Aphysical
19615732
SVIP_HUMANSVIPphysical
19615732
WAC_HUMANWACphysical
21811234
TERA_HUMANVCPphysical
21811234
STX5_HUMANSTX5physical
12473691
LARP7_HUMANLARP7physical
22863883
TERA_HUMANVCPphysical
23500464
WAC_HUMANWACphysical
23500464
UBC_HUMANUBCphysical
23500464
UBC_HUMANUBCphysical
23827681
TERA_HUMANVCPphysical
24163436
ZEB1_HUMANZEB1physical
29119051

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 VCIP1_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-408, AND MASS SPECTROMETRY.
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-1198, AND MASSSPECTROMETRY.
"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-747; SER-757; THR-761AND TYR-767, 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-747; SER-757; THR-763;THR-770; SER-994; SER-998 AND SER-1198, AND MASS SPECTROMETRY.
"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-747, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-870, AND MASSSPECTROMETRY.

TOP