UBN2_MOUSE - dbPTM
UBN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBN2_MOUSE
UniProt AC Q80WC1
Protein Name Ubinuclein-2
Gene Name Ubn2
Organism Mus musculus (Mouse).
Sequence Length 1314
Subcellular Localization
Protein Description
Protein Sequence MAEPRRVAFISLSPVRRREADFAGAEREPPRLEPQPYREPARAEPAPRADAQPPARDKPLPQREVSRAEPPMALQREPPRPEPPPPPLPLQTPPPRESASRAEPPPRPPKETVRLELVLKDPTDESCVEFSYPELLLCGEQRKKLVHTEDPFTDEHKERQEVEMLAKKFEMKYGGKARKHRKDRLQDLIDIGFGYDETDPFIDNSEAYDELVPASLTTKYGGFYINTGTLQFRQASDTEEDDFTDNQKHKPPKVPKIKEDDIEVKKRKRKEEGEKEKKPRKKVPKQLGVVALNSHKSEKKKKRYKDSLSLAAMIRKFQKEKDALKKESTPKVPVTPSSSSLPKPPCVTTALGDDIPDLGLNSADPDLPIFVSTNEHELFQEAENALEMLDDFDFDRLLDATSDGSPLSESGGENGNTTHPTFPSQVVPKVVPTLPEGLPVLLEKRIEDLRVAAKLFDEEGRKKFFTQDMNNILLDIELQLQELGPVIRSGVYSHLEAFVPCNKETLVKRLKKLHLNVQDDRLREPLQKLKLAVSNVMPEQLFKYQEDCQARSQAKCAKLQADEEREKNGSDDDDDEKPGKRVIGPRKKFHWDDTIRTLLCNLVEIKLGCYELEPNKSQSAEDYLKSFMETEVKPLWPKGWMQARMLFKESRSVHNHLTSAPAKKKVIPASKPKVKECSPKKDPKAPASVVASGGGPSTSSSTSIVASASSSSAPAQETICLDDSLDEDLSFPSASLDLVSEALAVINNGNKGPSVGSRLNVPTTKPRPGLREEKLASIMSKLPLATPKKLDSTQTAHSSSLIAGHTGPVPKKPQDLAHTGISSGLIAGSSIQNPKVSLEPLPARLLQQGLQRSSQIHASSSSQTHVSSSQAQAAASSHALGTSEAQDASSLTQVTKVHQHSAVQQNYVSPLQATISKSQTNPVVKLSNNPQLSCSSQLLKTSDKPLMYRLPLSTPSPGNGSQGPHPLVSRTAPSTTTSSNYLAKAMVSQISTQGFKSPFSMAASPKLAASPKPATSPKPLPSPKPSVSPKPSLSAKPSISTKQISKSNPAPKPAVCPSSSSPNTLVAQSSHSTSNNPVHKQPSGMNISRQSPTLNLLPSNRTSGLPTTKTLQAPSKLTNSSSTGTAGKNSLSGIPMNVPASRGSNLNSSGANRTSLSGGTGSGTQGATKPLSTPHRPTSASGSSVVTASVQSTAGASLLANASPLTLMTSPLSVTNQTVTPFGMLGGLVPVTMPFQFPLELLGFGTDTAGVTATSGSTSAALHHSLTQNLLKSLQPGAQHAAALPHSPLPAHLQQAFNDGGQSKGDTKLPRKPQ
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
11PhosphorylationPRRVAFISLSPVRRR
CCEEEEEECCCCCCC
19.1525159016
13PhosphorylationRVAFISLSPVRRREA
EEEEEECCCCCCCCC
17.9823527152
227PhosphorylationYGGFYINTGTLQFRQ
ECCEEEECCEEEEEE
23.2226643407
229PhosphorylationGFYINTGTLQFRQAS
CEEEECCEEEEEECC
18.4926643407
236PhosphorylationTLQFRQASDTEEDDF
EEEEEECCCCCCCCC
36.4125521595
238PhosphorylationQFRQASDTEEDDFTD
EEEECCCCCCCCCCC
38.4925521595
244PhosphorylationDTEEDDFTDNQKHKP
CCCCCCCCCCCCCCC
40.8226643407
265AcetylationKEDDIEVKKRKRKEE
CHHHHHHHHHHHHHH
33.797711939
282UbiquitinationKEKKPRKKVPKQLGV
HCCCCCCCCCHHHCC
66.12-
285UbiquitinationKPRKKVPKQLGVVAL
CCCCCCCHHHCCHHC
62.23-
296UbiquitinationVVALNSHKSEKKKKR
CHHCCCCCCHHHHHH
61.19-
297PhosphorylationVALNSHKSEKKKKRY
HHCCCCCCHHHHHHH
49.58-
304PhosphorylationSEKKKKRYKDSLSLA
CHHHHHHHHHHHHHH
28.2028059163
307PhosphorylationKKKRYKDSLSLAAMI
HHHHHHHHHHHHHHH
18.7328059163
402PhosphorylationDRLLDATSDGSPLSE
HHHHHCCCCCCCCCC
41.5122817900
405PhosphorylationLDATSDGSPLSESGG
HHCCCCCCCCCCCCC
27.8822817900
408PhosphorylationTSDGSPLSESGGENG
CCCCCCCCCCCCCCC
32.8522817900
410PhosphorylationDGSPLSESGGENGNT
CCCCCCCCCCCCCCC
49.0425293948
417PhosphorylationSGGENGNTTHPTFPS
CCCCCCCCCCCCCHH
28.0728576409
418PhosphorylationGGENGNTTHPTFPSQ
CCCCCCCCCCCCHHH
29.8328576409
421PhosphorylationNGNTTHPTFPSQVVP
CCCCCCCCCHHHHCC
40.3428576409
570PhosphorylationEEREKNGSDDDDDEK
HHHHHCCCCCCCCCC
47.4625266776
617PhosphorylationYELEPNKSQSAEDYL
EECCCCCCCCHHHHH
35.6927841257
678PhosphorylationKPKVKECSPKKDPKA
CCCCCCCCCCCCCCC
40.6326745281
763PhosphorylationGSRLNVPTTKPRPGL
CCCCCCCCCCCCCCC
43.0730482847
780PhosphorylationEKLASIMSKLPLATP
HHHHHHHHCCCCCCC
29.3927600695
806PhosphorylationSSLIAGHTGPVPKKP
CCCCCCCCCCCCCCH
42.11-
909PhosphorylationAVQQNYVSPLQATIS
HHHHCCCCCHHHCCC
14.99-
944AcetylationQLLKTSDKPLMYRLP
HHHHCCCCCEEEEEE
39.5623806337
1004PhosphorylationSPFSMAASPKLAASP
CCCCCCCCCCCCCCC
17.0326643407
1010PhosphorylationASPKLAASPKPATSP
CCCCCCCCCCCCCCC
28.0528066266
1015PhosphorylationAASPKPATSPKPLPS
CCCCCCCCCCCCCCC
54.8328066266
1016PhosphorylationASPKPATSPKPLPSP
CCCCCCCCCCCCCCC
32.7928066266
1026PhosphorylationPLPSPKPSVSPKPSL
CCCCCCCCCCCCCCC
41.1628066266
1028PhosphorylationPSPKPSVSPKPSLSA
CCCCCCCCCCCCCCC
31.3828066266
1032PhosphorylationPSVSPKPSLSAKPSI
CCCCCCCCCCCCCCC
40.8728066266
1034PhosphorylationVSPKPSLSAKPSIST
CCCCCCCCCCCCCCH
38.2928066266
1036AcetylationPKPSLSAKPSISTKQ
CCCCCCCCCCCCHHH
35.6023806337
1045PhosphorylationSISTKQISKSNPAPK
CCCHHHHCCCCCCCC
27.7726745281
1047PhosphorylationSTKQISKSNPAPKPA
CHHHHCCCCCCCCCC
41.0526745281
1069PhosphorylationPNTLVAQSSHSTSNN
CCCEEEECCCCCCCC
21.9322802335
1070PhosphorylationNTLVAQSSHSTSNNP
CCEEEECCCCCCCCC
14.9122802335
1072PhosphorylationLVAQSSHSTSNNPVH
EEEECCCCCCCCCCC
35.1622802335
1073PhosphorylationVAQSSHSTSNNPVHK
EEECCCCCCCCCCCC
30.0122802335
1074PhosphorylationAQSSHSTSNNPVHKQ
EECCCCCCCCCCCCC
37.3122802335
1083PhosphorylationNPVHKQPSGMNISRQ
CCCCCCCCCCCCCCC
48.4522802335
1088PhosphorylationQPSGMNISRQSPTLN
CCCCCCCCCCCCCCC
21.1822802335
1091PhosphorylationGMNISRQSPTLNLLP
CCCCCCCCCCCCCCC
20.8120469934
1093PhosphorylationNISRQSPTLNLLPSN
CCCCCCCCCCCCCCC
33.2629472430
1116AcetylationKTLQAPSKLTNSSST
CCCCCCCCCCCCCCC
59.27-

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 UBN2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBN2_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 UBN2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBN2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASSSPECTROMETRY.

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