SCAP_MOUSE - dbPTM
SCAP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAP_MOUSE
UniProt AC Q6GQT6
Protein Name Sterol regulatory element-binding protein cleavage-activating protein
Gene Name Scap {ECO:0000312|MGI:MGI:2135958}
Organism Mus musculus (Mouse).
Sequence Length 1276
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane
Multi-pass membrane protein . Moves from the endoplasmic reticulum to the Gol
Protein Description Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP/SREBF complex from the ER upon low cholesterol. Formation of a ternary complex with INSIG at high sterol concentrations leads to masking of an ER-export signal in SCAP and retention of the complex in the ER. Low sterol concentrations trigger release of INSIG, a conformational change in the SSC domain of SCAP, unmasking of the ER export signal, recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of SREBF in the Golgi, release of the transcription factor fragment of SREBF from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway..
Protein Sequence MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKGYSPPPADSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHRNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRSLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNAATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQQAVRPSTPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASHPDPAFSIFPPDAPKLPENQTLPGELPEHAGPAEGVHDSRAPEVTWGPEDEELWRKLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLHLNPREALEGRHPQDGRSAWAPQEPLPAGLWESGPKGPGGTQTHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGPGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGPRRDSCGGGAFETQENWERLSDGGKASPEEPGDSPPLRRRPRGPPPPSLFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRVGCGRSRDSGYDFSRLVQRVYQEEGLAAMRMPALRPPSPGPPLPQASQEEGTAPEKGSPPLAWTPSTAGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSNEEISSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSSVYSSSNTVTCHRTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLDDSCCLFTLKGHSGAITAVYIDQTMVLASGGQDGAICLWDVLTGSRVSQTFAHRGDVTSLTCTASCVISSGLDDFISIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
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
52PhosphorylationLKLPLPGTGPVEFST
HCCCCCCCCCCCCCC
36.0528059163
208PhosphorylationKTLQTSATLKDLLFG
CCCCCCCCHHHHHHC
33.8223140645
249PhosphorylationRYHAKFLSSLRARLM
HHHHHHHHHHHHHHH
30.3825159016
250PhosphorylationYHAKFLSSLRARLML
HHHHHHHHHHHHHHH
24.8325159016
263N-linked_GlycosylationMLLHPSPNCSLRAEN
HHHCCCCCCCCCCCC
32.14-
454UbiquitinationMELADLNKRLPPESC
HHHHHHHHCCCHHHH
63.71PubMed
466UbiquitinationESCLPSAKPVGRPAR
HHHCCCCCCCCCCCC
44.57PubMed
483PhosphorylationRQQAVRPSTPHTITL
HHHCCCCCCCCEEEE
43.9623140645
484PhosphorylationQQAVRPSTPHTITLQ
HHCCCCCCCCEEEEC
23.0523140645
487PhosphorylationVRPSTPHTITLQPSS
CCCCCCCEEEECCHH
19.5022871156
590N-linked_GlycosylationDAPKLPENQTLPGEL
CCCCCCCCCCCCCCC
37.89-
641N-linked_GlycosylationPTLFNYYNITLAKRY
CHHHHHCCHHHHHHH
15.48-
730PhosphorylationVLLLLCLYRVLCPRN
HHHHHHHHHHHCCCC
9.55-
755S-palmitoylationRRRGELPCDDYGYAP
CCCCCCCCCCCCCCC
10.9928680068
821PhosphorylationRPGPRRDSCGGGAFE
CCCCCCCCCCCCCCC
16.9225521595
829PhosphorylationCGGGAFETQENWERL
CCCCCCCCHHHHHHH
34.4323984901
837PhosphorylationQENWERLSDGGKASP
HHHHHHHCCCCCCCC
40.1925159016
843PhosphorylationLSDGGKASPEEPGDS
HCCCCCCCCCCCCCC
36.0127818261
850PhosphorylationSPEEPGDSPPLRRRP
CCCCCCCCCCCCCCC
34.0425521595
905PhosphorylationGCGRSRDSGYDFSRL
CCCCCCCCCCCHHHH
37.8425266776
907PhosphorylationGRSRDSGYDFSRLVQ
CCCCCCCCCHHHHHH
20.1226643407
934PhosphorylationMPALRPPSPGPPLPQ
CCCCCCCCCCCCCCC
45.2126824392
943PhosphorylationGPPLPQASQEEGTAP
CCCCCCCCCCCCCCC
32.6425159016
948PhosphorylationQASQEEGTAPEKGSP
CCCCCCCCCCCCCCC
42.1726643407
1030PhosphorylationNGSLDFFSLETHTSL
CCCCEEEEEEECCCC
25.8626643407
1033PhosphorylationLDFFSLETHTSLSPL
CEEEEEEECCCCCCE
35.4326643407
1035PhosphorylationFFSLETHTSLSPLQF
EEEEEECCCCCCEEE
38.4926643407
1036PhosphorylationFSLETHTSLSPLQFR
EEEEECCCCCCEEEC
21.1726643407
1038PhosphorylationLETHTSLSPLQFRGT
EEECCCCCCEEECCC
24.2726643407
1045PhosphorylationSPLQFRGTPGRGSSP
CCEEECCCCCCCCCC
20.5026643407
1048MethylationQFRGTPGRGSSPSSS
EECCCCCCCCCCCCC
42.9224129315
1050PhosphorylationRGTPGRGSSPSSSVY
CCCCCCCCCCCCCCC
37.4025266776
1051PhosphorylationGTPGRGSSPSSSVYS
CCCCCCCCCCCCCCC
31.4625266776
1053PhosphorylationPGRGSSPSSSVYSSS
CCCCCCCCCCCCCCC
36.8726643407
1054PhosphorylationGRGSSPSSSVYSSSN
CCCCCCCCCCCCCCC
27.4926643407
1055PhosphorylationRGSSPSSSVYSSSNT
CCCCCCCCCCCCCCE
29.4326643407
1057PhosphorylationSSPSSSVYSSSNTVT
CCCCCCCCCCCCEEE
12.5626643407
1058PhosphorylationSPSSSVYSSSNTVTC
CCCCCCCCCCCEEEE
25.7426643407
1060PhosphorylationSSSVYSSSNTVTCHR
CCCCCCCCCEEEEEE
30.4926643407
1111PhosphorylationDDSCCLFTLKGHSGA
CCCEEEEEECCCCCC
18.0222871156

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 SCAP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
454Kubiquitylation

29068315
466Kubiquitylation

29068315

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 SCAP_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INSI1_HUMANINSIG1physical
12202038
SRBP2_HUMANSREBF2physical
12202038

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

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Related Literatures of Post-Translational Modification

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