SCEL_HUMAN - dbPTM
SCEL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCEL_HUMAN
UniProt AC O95171
Protein Name Sciellin
Gene Name SCEL
Organism Homo sapiens (Human).
Sequence Length 688
Subcellular Localization Cytoplasm. Membrane. May become cross-linked to membrane proteins by transglutaminase.
Protein Description May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope..
Protein Sequence MSNVTLRKMSPTGNEMKSTTQGTTRKQQDFHEVNKRRTFLQDNSWIKKRPEEEKDENYGRVVLNRHNSHDALDRKVNERDVPKATISRYSSDDTLDRISDRNDAAKTYKANTLDNQLTNRSMSMFRSLEVTKLQPGGSLNANTSNTIASTSATTPVKKKRQSWFPPPPPGYNASSSTGTRRREPGVHPPIPPKPSSPVSSPNQLRQDNRQIHPPKPGVYTETNRSAERNIRSQDLDNIVKVATSLQRSDKGEELDNLIKMNKSLNRNQGLDSLFRANPKVEEREKRAKSLESLIYMSTRTDKDGKGIQSLGSPIKVNQRTDKNEKGRQNLESVAKVNARMNKTSRRSEDLDNATEVNPKGHENTTGKKDLDGLIKVDPETNKNITRGQSLDNLIKVTPEVKRSNQGSKDLNNFIKVYPGTEKSTEGGQSLDSLIKVTPERNRTNQGNQDLENLIKVIPSANKSSEQGLDEHINVSPKAVKNTDGKQDLDKLIKVNPEIFTNNQRNQDLANLIKVNPAVIRNNQSQDLDNLIKVKPSALRNTNRDQNLENLIEVNSHVSENKNGSSNTGAKQAGPQDTVVYTRTYVENSKSPKDGYQENISGKYIQTVYSTSDRSVIERDMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKQPLENLQAGDSIWIYRQTIHCEPCYSKIMAKWIP
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
10PhosphorylationNVTLRKMSPTGNEMK
CCEEEECCCCCCCCC
23.5025394399
12PhosphorylationTLRKMSPTGNEMKST
EEEECCCCCCCCCCC
45.3822617229
18PhosphorylationPTGNEMKSTTQGTTR
CCCCCCCCCCCCCCH
35.06-
38PhosphorylationHEVNKRRTFLQDNSW
HHHHHHHHHHCCCCH
32.5026074081
44PhosphorylationRTFLQDNSWIKKRPE
HHHHCCCCHHHCCCH
38.1726074081
58PhosphorylationEEEKDENYGRVVLNR
HHHCCCCCCEEEECC
12.3125394399
68PhosphorylationVVLNRHNSHDALDRK
EEECCCCCCHHHHHC
19.3328355574
83AcetylationVNERDVPKATISRYS
CCCCCCCHHHHCCCC
58.99-
85PhosphorylationERDVPKATISRYSSD
CCCCCHHHHCCCCCC
26.1323663014
87PhosphorylationDVPKATISRYSSDDT
CCCHHHHCCCCCCCH
22.3223663014
89PhosphorylationPKATISRYSSDDTLD
CHHHHCCCCCCCHHH
13.0223663014
90PhosphorylationKATISRYSSDDTLDR
HHHHCCCCCCCHHHH
26.6122617229
91PhosphorylationATISRYSSDDTLDRI
HHHCCCCCCCHHHHH
30.4828355574
94PhosphorylationSRYSSDDTLDRISDR
CCCCCCCHHHHHHCC
35.2323663014
99PhosphorylationDDTLDRISDRNDAAK
CCHHHHHHCCCHHHH
31.2630183078
108PhosphorylationRNDAAKTYKANTLDN
CCHHHHHHHHCHHHH
13.8520049867
109MethylationNDAAKTYKANTLDNQ
CHHHHHHHHCHHHHH
40.15-
112PhosphorylationAKTYKANTLDNQLTN
HHHHHHCHHHHHHHH
40.1127966365
121PhosphorylationDNQLTNRSMSMFRSL
HHHHHHHHHHHHHHE
19.7822617229
123PhosphorylationQLTNRSMSMFRSLEV
HHHHHHHHHHHHEEE
18.9323898821
127PhosphorylationRSMSMFRSLEVTKLQ
HHHHHHHHEEEEEEC
20.0222617229
143PhosphorylationGGSLNANTSNTIAST
CCCCCCCCCCCCCCC
22.4223090842
144PhosphorylationGSLNANTSNTIASTS
CCCCCCCCCCCCCCC
31.6123090842
149PhosphorylationNTSNTIASTSATTPV
CCCCCCCCCCCCCCC
21.0325404012
150PhosphorylationTSNTIASTSATTPVK
CCCCCCCCCCCCCCC
17.2327251275
151PhosphorylationSNTIASTSATTPVKK
CCCCCCCCCCCCCCC
22.5627251275
153PhosphorylationTIASTSATTPVKKKR
CCCCCCCCCCCCCCC
31.2523090842
154PhosphorylationIASTSATTPVKKKRQ
CCCCCCCCCCCCCCC
26.2925394399
162PhosphorylationPVKKKRQSWFPPPPP
CCCCCCCCCCCCCCC
34.4223898821
195PhosphorylationPPIPPKPSSPVSSPN
CCCCCCCCCCCCCHH
54.0930266825
196PhosphorylationPIPPKPSSPVSSPNQ
CCCCCCCCCCCCHHH
37.5430266825
199PhosphorylationPKPSSPVSSPNQLRQ
CCCCCCCCCHHHHCC
43.3830266825
200PhosphorylationKPSSPVSSPNQLRQD
CCCCCCCCHHHHCCC
28.2730266825
219PhosphorylationHPPKPGVYTETNRSA
CCCCCCCCCCCCCHH
12.5528152594
220PhosphorylationPPKPGVYTETNRSAE
CCCCCCCCCCCCHHH
33.6528152594
222PhosphorylationKPGVYTETNRSAERN
CCCCCCCCCCHHHHH
28.2928152594
225PhosphorylationVYTETNRSAERNIRS
CCCCCCCHHHHHHHH
36.2323898821
232PhosphorylationSAERNIRSQDLDNIV
HHHHHHHHHCHHHHH
25.0129460479
243 (in isoform 2)Phosphorylation-32.7225056879
263PhosphorylationNLIKMNKSLNRNQGL
HHHHHHHHCCCCCCH
26.3522617229
272PhosphorylationNRNQGLDSLFRANPK
CCCCCHHHHHHHCHH
34.1525404012
289PhosphorylationEREKRAKSLESLIYM
HHHHHHHHHHHHHHH
36.0628355574
292PhosphorylationKRAKSLESLIYMSTR
HHHHHHHHHHHHHHC
25.9230206219
295PhosphorylationKSLESLIYMSTRTDK
HHHHHHHHHHHCCCC
7.1222617229
297PhosphorylationLESLIYMSTRTDKDG
HHHHHHHHHCCCCCC
9.5830206219
298PhosphorylationESLIYMSTRTDKDGK
HHHHHHHHCCCCCCC
22.5123312004
300PhosphorylationLIYMSTRTDKDGKGI
HHHHHHCCCCCCCCH
47.71-
309PhosphorylationKDGKGIQSLGSPIKV
CCCCCHHHCCCCEEC
32.5530266825
312PhosphorylationKGIQSLGSPIKVNQR
CCHHHCCCCEECCCC
28.8430266825
332PhosphorylationKGRQNLESVAKVNAR
HHHHHHHHHHHHHHH
30.4624719451
343PhosphorylationVNARMNKTSRRSEDL
HHHHCCCCCCCCHHC
23.5927966365
344PhosphorylationNARMNKTSRRSEDLD
HHHCCCCCCCCHHCC
27.5725394399
347PhosphorylationMNKTSRRSEDLDNAT
CCCCCCCCHHCCCCC
34.0622617229
354PhosphorylationSEDLDNATEVNPKGH
CHHCCCCCCCCCCCC
46.8823312004
385PhosphorylationPETNKNITRGQSLDN
CCCCCCCCCCCCHHH
37.8322617229
389PhosphorylationKNITRGQSLDNLIKV
CCCCCCCCHHHHHHH
40.2830266825
397PhosphorylationLDNLIKVTPEVKRSN
HHHHHHHCHHHHHCC
14.5530266825
417PhosphorylationLNNFIKVYPGTEKST
HHHCEEECCCCCCCC
7.3128152594
432PhosphorylationEGGQSLDSLIKVTPE
CCCCCHHHHEECCCC
36.9724719451
433PhosphorylationGGQSLDSLIKVTPER
CCCCHHHHEECCCCC
4.3633259812
437PhosphorylationLDSLIKVTPERNRTN
HHHHEECCCCCCCCC
17.9030266825
443PhosphorylationVTPERNRTNQGNQDL
CCCCCCCCCCCCCCH
35.1323898821
455PhosphorylationQDLENLIKVIPSANK
CCHHHHHHHCCCCCC
36.9633259812
463PhosphorylationVIPSANKSSEQGLDE
HCCCCCCCCCCCHHH
38.6323927012
464PhosphorylationIPSANKSSEQGLDEH
CCCCCCCCCCCHHHH
35.2323927012
475PhosphorylationLDEHINVSPKAVKNT
HHHHCCCCHHHHHCC
19.0530266825
490TrimethylationDGKQDLDKLIKVNPE
CCCCCHHHHHHCCHH
60.45-
490MethylationDGKQDLDKLIKVNPE
CCCCCHHHHHHCCHH
60.4524129315
524PhosphorylationAVIRNNQSQDLDNLI
HHHCCCCCCCHHHHH
27.9925056879
558PhosphorylationIEVNSHVSENKNGSS
HHHHHHHCCCCCCCC
29.99-
564PhosphorylationVSENKNGSSNTGAKQ
HCCCCCCCCCCCCCC
29.79-
567PhosphorylationNKNGSSNTGAKQAGP
CCCCCCCCCCCCCCC
40.23-
580PhosphorylationGPQDTVVYTRTYVEN
CCCCEEEEEEEEECC
6.0325394399
581PhosphorylationPQDTVVYTRTYVENS
CCCEEEEEEEEECCC
12.6228152594
583PhosphorylationDTVVYTRTYVENSKS
CEEEEEEEEECCCCC
24.9027794612
584PhosphorylationTVVYTRTYVENSKSP
EEEEEEEEECCCCCC
11.5027794612
588PhosphorylationTRTYVENSKSPKDGY
EEEEECCCCCCCCCC
22.4722617229
590PhosphorylationTYVENSKSPKDGYQE
EEECCCCCCCCCCCC
36.6822617229
595PhosphorylationSKSPKDGYQENISGK
CCCCCCCCCCCCCCC
23.8428152594
603PhosphorylationQENISGKYIQTVYST
CCCCCCCEEEEEECC
11.2028152594
608PhosphorylationGKYIQTVYSTSDRSV
CCEEEEEECCCCCHH
15.0425394399
609PhosphorylationKYIQTVYSTSDRSVI
CEEEEEECCCCCHHH
19.6628152594
623PhosphorylationIERDMCTYCRKPLGV
HHHHHHHHCCCCCCC
5.82-
665PhosphorylationENLQAGDSIWIYRQT
HHCCCCCEEEEEEEE
20.92-
669PhosphorylationAGDSIWIYRQTIHCE
CCCEEEEEEEEEECC
5.0119060867
679PhosphorylationTIHCEPCYSKIMAKW
EEECCCCHHHHHHHC
24.5828152594
680PhosphorylationIHCEPCYSKIMAKWI
EECCCCHHHHHHHCC
23.5628152594

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 SCEL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCEL_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 SCEL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TXNIP_HUMANTXNIPphysical
14632196
A4_HUMANAPPphysical
21832049
NMI_HUMANNMIphysical
25416956
FXR2_HUMANFXR2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
TSG10_HUMANTSGA10physical
25416956
NMI_HUMANNMIphysical
21516116
RB11B_HUMANRAB11Bphysical
28514442

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 SCEL_HUMAN

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Related Literatures of Post-Translational Modification

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