SEBP2_HUMAN - dbPTM
SEBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEBP2_HUMAN
UniProt AC Q96T21
Protein Name Selenocysteine insertion sequence-binding protein 2
Gene Name SECISBP2
Organism Homo sapiens (Human).
Sequence Length 854
Subcellular Localization Isoform 1: Nucleus .
Isoform 2: Mitochondrion .
Protein Description Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB..
Protein Sequence MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVTEQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYRGFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHHLSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQPKWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPMGYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHPTQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRDRIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL
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
2Acetylation------MASEGPREP
------CCCCCCCCC
19.11-
15AcetylationEPESEGIKLSADVKP
CCCCCCCCCCCCCCC
47.4412433889
21UbiquitinationIKLSADVKPFVPRFA
CCCCCCCCCCCCCCC
33.03-
26MethylationDVKPFVPRFAGLNVA
CCCCCCCCCCCCEEE
28.84115493599
58UbiquitinationYPFVQEPPVTEQKIY
CCCCCCCCCCCCEEE
44.93-
60PhosphorylationFVQEPPVTEQKIYTE
CCCCCCCCCCEEECC
38.1729759185
65PhosphorylationPVTEQKIYTEDMAFG
CCCCCEEECCCCCCC
15.8829759185
66PhosphorylationVTEQKIYTEDMAFGA
CCCCEEECCCCCCCC
29.0529759185
90UbiquitinationSEITLHPYAYSPYTL
CCEEECCCCCCCCCC
13.87-
105UbiquitinationDSTQNVYSVPGSQYL
CCCCCEEECCHHHHH
19.97-
126UbiquitinationYRGFQTVKHRNENTC
HCCCCCCCCCCCCCC
39.99-
140UbiquitinationCPLPQEMKALFKKKT
CCCCHHHHHHHCCCC
40.98-
158UbiquitinationKKTYDQQKFDSERAD
CCCCCHHHHCHHHCC
45.57-
173UbiquitinationGTISSEIKSARGSHH
CCCHHHHHHCCCCCC
33.73-
174PhosphorylationTISSEIKSARGSHHL
CCHHHHHHCCCCCCE
28.9420044836
176MethylationSSEIKSARGSHHLSI
HHHHHHCCCCCCEEE
54.99115493607
184PhosphorylationGSHHLSIYAENSLKS
CCCCEEEEEECCCCC
12.4125159151
199UbiquitinationDGYHKRTDRKSRIIA
CCCCCCCCCCCCEEE
61.10-
238UbiquitinationNNMSEIQKQPKWGPV
CCHHHHHHCCCCCCC
74.38-
247PhosphorylationPKWGPVHSVSTDISL
CCCCCCCCCCCCHHH
20.2823186163
249PhosphorylationWGPVHSVSTDISLLR
CCCCCCCCCCHHHHH
24.3125954137
250PhosphorylationGPVHSVSTDISLLRE
CCCCCCCCCHHHHHH
34.8925954137
253PhosphorylationHSVSTDISLLREVVK
CCCCCCHHHHHHHHC
24.9423186163
260UbiquitinationSLLREVVKPAAVLSK
HHHHHHHCHHHEECC
33.83-
267UbiquitinationKPAAVLSKGEIVVKN
CHHHEECCCEEEECC
57.30-
273UbiquitinationSKGEIVVKNNPNESV
CCCEEEECCCCCCCC
39.86-
285UbiquitinationESVTANAATNSPSCT
CCCEEECCCCCCCCC
13.71-
286PhosphorylationSVTANAATNSPSCTR
CCEEECCCCCCCCCC
33.5425159151
288PhosphorylationTANAATNSPSCTREL
EEECCCCCCCCCCEE
17.5225159151
290PhosphorylationNAATNSPSCTRELSW
ECCCCCCCCCCEECC
28.1321712546
292PhosphorylationATNSPSCTRELSWTP
CCCCCCCCCEECCCC
31.3629978859
296PhosphorylationPSCTRELSWTPMGYV
CCCCCEECCCCCCCC
24.9328857561
307PhosphorylationMGYVVRQTLSTELSA
CCCCHHHHHCHHHCC
16.47-
326UbiquitinationVTSMINLKTIASSAD
CCCCEEHHHHHCCCC
33.14-
335UbiquitinationIASSADPKNVSIPSS
HHCCCCCCCCCCCCH
71.21-
338PhosphorylationSADPKNVSIPSSEAL
CCCCCCCCCCCHHHH
37.8729978859
341PhosphorylationPKNVSIPSSEALSSD
CCCCCCCCHHHHCCC
38.8629978859
341O-linked_GlycosylationPKNVSIPSSEALSSD
CCCCCCCCHHHHCCC
38.8630379171
342PhosphorylationKNVSIPSSEALSSDP
CCCCCCCHHHHCCCC
22.8728985074
346PhosphorylationIPSSEALSSDPSYNK
CCCHHHHCCCCCCCC
39.4829978859
347PhosphorylationPSSEALSSDPSYNKE
CCHHHHCCCCCCCCC
55.1629978859
350PhosphorylationEALSSDPSYNKEKHI
HHHCCCCCCCCCCCC
46.4529978859
351PhosphorylationALSSDPSYNKEKHII
HHCCCCCCCCCCCCC
35.3229978859
353UbiquitinationSSDPSYNKEKHIIHP
CCCCCCCCCCCCCCH
60.96-
355UbiquitinationDPSYNKEKHIIHPTQ
CCCCCCCCCCCCHHH
41.53-
361PhosphorylationEKHIIHPTQKSKASQ
CCCCCCHHHHCCCCC
34.1725690035
364PhosphorylationIIHPTQKSKASQGSD
CCCHHHHCCCCCCCH
24.5225247763
367PhosphorylationPTQKSKASQGSDLEQ
HHHHCCCCCCCHHHH
38.5230108239
370PhosphorylationKSKASQGSDLEQNEA
HCCCCCCCHHHHHHH
31.2425159151
378PhosphorylationDLEQNEASRKNKKKK
HHHHHHHHHHHHHHH
37.2921406692
384UbiquitinationASRKNKKKKEKSTSK
HHHHHHHHHCCCCCC
68.71-
388PhosphorylationNKKKKEKSTSKYEVL
HHHHHCCCCCCCEEE
38.7226657352
392PhosphorylationKEKSTSKYEVLTVQE
HCCCCCCCEEEECCC
15.8428796482
396PhosphorylationTSKYEVLTVQEPPRI
CCCCEEEECCCCCCC
25.8928796482
424PhosphorylationERRDRIETPKFQSKQ
HHHHCCCCCCCCCCC
29.4329978859
429PhosphorylationIETPKFQSKQQPQDN
CCCCCCCCCCCCCCC
35.2529978859
499PhosphorylationGERGRRMSQMKTPHN
CCCHHCHHHCCCCCC
25.8824719451
533AcetylationAKKPTSLKKIILKER
CCCCCCHHHHHHHHH
41.5124431589
609PhosphorylationGTELQRDTEASHLAP
CCCCCCCCHHHHCCC
35.3224732914
612PhosphorylationLQRDTEASHLAPNHT
CCCCCHHHHCCCCCC
16.8924732914
619PhosphorylationSHLAPNHTTFPKIHS
HHCCCCCCCCCCHHH
36.4524732914
620PhosphorylationHLAPNHTTFPKIHSR
HCCCCCCCCCCHHHH
30.3224732914
632UbiquitinationHSRRFRDYCSQMLSK
HHHHHHHHHHHHHHH
6.97-
646PhosphorylationKEVDACVTDLLKELV
HHHHHHHHHHHHHHH
22.3328258704
650UbiquitinationACVTDLLKELVRFQD
HHHHHHHHHHHHHHH
57.19-
660PhosphorylationVRFQDRMYQKDPVKA
HHHHHHHHCCCCCCH
17.1918083107
662UbiquitinationFQDRMYQKDPVKAKT
HHHHHHCCCCCCHHH
46.65-
803GlutathionylationLPTQGPSCPAEDGPP
CCCCCCCCCCCCCCC
4.1022833525
815UbiquitinationGPPALKEKEEPHYIE
CCCCCCCCCCCCHHH
66.83-
820PhosphorylationKEKEEPHYIEIWKKH
CCCCCCCHHHHHHHH
15.8028796482

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 SEBP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEBP2_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 SEBP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609698Abnormal thyroid hormone metabolism (ATHYHM)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SEBP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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