SCAP_CRIGR - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCAP_CRIGR
• UniProt AC: P97260
• Protein Name: Sterol regulatory element-binding protein cleavage-activating protein
• Gene Name: SCAP
• Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
• 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 Golgi in
• 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: MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKDYSPPPVDSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHKNLLAVDVFRLPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRNLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRTVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNVATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMFFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQLAVRPAMPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASRPDPAFSIFPPDAPKLPENQTVPGELPEHAAPAEGVHDSRAPEVTWGPEDEELWRRLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLRLNPQEALEGRQPQDGRSAWAPPESLPAGLWEAGPKGPGGTQAHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGAGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGSRRDSCGGGAFETQENWERLSDGGKTSPEEPGESPPLRHRPRGPPQPALFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRAGCGRARDSGYDFSRLVQRVYQEEGLAAVRMPALRPPSPGSPLPQASQEDGAAPEKGSPPLAWAPSTAGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSNDEVSSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSSVYSSSNTVACHLTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHTFAHRGDVTSLTCTTSCVISSGLDDLINIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD

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
263	N-linked_Glycosylation	MLLHPSPNCSLRAEN HHHCCCCCCCCCEEC	32.14	9642295
590	N-linked_Glycosylation	DAPKLPENQTVPGEL CCCCCCCCCCCCCCC	40.66	9642295
641	N-linked_Glycosylation	PTLFNYYNITLAKRY CHHHHHCCHHHHHHH	15.48	9642295
821	Phosphorylation	RPGSRRDSCGGGAFE CCCCCCCCCCCCCCC	16.92	-
837	Phosphorylation	QENWERLSDGGKTSP HHHHEECCCCCCCCC	40.19	-
843	Phosphorylation	LSDGGKTSPEEPGES CCCCCCCCCCCCCCC	33.52	-
850	Phosphorylation	SPEEPGESPPLRHRP CCCCCCCCCCCCCCC	37.42	-
905	Phosphorylation	GCGRARDSGYDFSRL CCCCCCCCCCCHHHH	33.43	-
934	Phosphorylation	MPALRPPSPGSPLPQ CCCCCCCCCCCCCCC	44.57	-
1048	Methylation	QFRGTPGRGSSPSSS EECCCCCCCCCCCCC	42.92	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SCAP_CRIGR !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SCAP_CRIGR !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SCAP_CRIGR !!

Protein-Protein Interaction

Oops, there are no PPI records of SCAP_CRIGR !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Topology of SREBP cleavage-activating protein, a polytopic membraneprotein with a sterol-sensing domain.";
Nohturfft A., Brown M.S., Goldstein J.L.;
J. Biol. Chem. 273:17243-17250(1998).
Cited for: TOPOLOGY, AND GLYCOSYLATION AT ASN-263; ASN-590 AND ASN-641.
PubMed: 9642295