SCAP_HUMAN - dbPTM
SCAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAP_HUMAN
UniProt AC Q12770
Protein Name Sterol regulatory element-binding protein cleavage-activating protein
Gene Name SCAP {ECO:0000312|HGNC:HGNC:30634}
Organism Homo sapiens (Human).
Sequence Length 1279
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 (By similarity)..
Protein Sequence MTLTERLREKISRAFYNHGLLCASYPIPIILFTGFCILACCYPLLKLPLPGTGPVEFTTPVKDYSPPPVDSDRKQGEPTEQPEWYVGAPVAYVQQIFVKSSVFPWHKNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGIRSLEELCLQVTDLLPGLRKLRNLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQHYHAKFLGSLRARLMLLHPSPNCSLRAESLVHVHFKEEIGVAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNMATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPEACLPSAKPVGQPTRYERQLAVRPSTPHTITLQPSSFRNLRLPKRLRVVYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRNYLAAQVTEQSPLGEGALAPMPVPSGMLPPSHPDPAFSIFPPDAPKLPENQTSPGESPERGGPAEVVHDSPVPEVTWGPEDEELWRKLSFRHWPTLFSYYNITLAKRYISLLPVIPVTLRLNPREALEGRHPQDGRSAWPPPGPIPAGHWEAGPKGPGGVQAHGDVTLYKVAALGLATGIVLVLLLLCLYRVLCPRNYGQLGGGPGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGHVCVWDAQTGDCLTRIPRPGRQRRDSGVGSGLEAQESWERLSDGGKAGPEEPGDSPPLRHRPRGPPPPSLFGDQPDLTCLIDTNFSAQPRSSQPTQPEPRHRAVCGRSRDSPGYDFSCLVQRVYQEEGLAAVCTPALRPPSPGPVLSQAPEDEGGSPEKGSPSLAWAPSAEGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSSEEVSSGITALVFLDKRIVAARLNGSLDFFSLETHTALSPLQFRGTPGRGSSPASPVYSSSDTVACHLTHTVPCAHQKPITALKAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHVFAHRGDVTSLTCTTSCVISSGLDDLISIWDRSTGIKFYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
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
2Phosphorylation------MTLTERLRE
------CCHHHHHHH		54.4129507054
4Phosphorylation----MTLTERLREKI
----CCHHHHHHHHH		26.8729507054
62 (in isoform 4)Ubiquitination-52.7521906983
81 (in isoform 2)Ubiquitination-43.6321906983
206PhosphorylationEPKTLQTSATLKDLL
CCCCCCCCCCHHHHH		13.2924114839
243PhosphorylationITLVFQHYHAKFLGS
HEEHHHHHHHHHHHH		7.8417053785
250PhosphorylationYHAKFLGSLRARLML
HHHHHHHHHHHHHHH		19.4824719451
263N-linked_GlycosylationMLLHPSPNCSLRAES
HHHCCCCCCCCCCEE		32.14UniProtKB CARBOHYD
265PhosphorylationLHPSPNCSLRAESLV
HCCCCCCCCCCEEEE		27.7724719451
378UbiquitinationTPVDLEVKLRIAQGL
CCCCHHHHHHHHCCC		23.75-
429 (in isoform 4)Phosphorylation-5.2625849741
433 (in isoform 4)Phosphorylation-3.7129507054
448 (in isoform 2)Phosphorylation-38.7125849741
450 (in isoform 4)Ubiquitination-13.1121906983
452 (in isoform 2)Phosphorylation-7.2829507054
454 (in isoform 1)Ubiquitination-63.7121906983
454UbiquitinationMELADLNKRLPPEAC
HHHHHHHHCCCHHHH		63.7121906983
454 (in isoform 3)Ubiquitination-63.7121906983
464PhosphorylationPPEACLPSAKPVGQP
CHHHHCCCCCCCCCC		35.6624719451
468 (in isoform 2)Ubiquitination-12.5521906983
483PhosphorylationRQLAVRPSTPHTITL
EEEEECCCCCCEEEE		43.9623312004
484PhosphorylationQLAVRPSTPHTITLQ
EEEECCCCCCEEEEC		23.0523312004
487PhosphorylationVRPSTPHTITLQPSS
ECCCCCCEEEECCHH		19.5023312004
489PhosphorylationPSTPHTITLQPSSFR
CCCCCEEEECCHHHC		22.0923312004
493PhosphorylationHTITLQPSSFRNLRL
CEEEECCHHHCCCCC		29.1923312004
494PhosphorylationTITLQPSSFRNLRLP
EEEECCHHHCCCCCC		34.6023312004
565O-linked_GlycosylationLAPMPVPSGMLPPSH
CCCCCCCCCCCCCCC		36.75OGP
571O-linked_GlycosylationPSGMLPPSHPDPAFS
CCCCCCCCCCCCCCC		45.79OGP
578O-linked_GlycosylationSHPDPAFSIFPPDAP
CCCCCCCCCCCCCCC		25.98OGP
590N-linked_GlycosylationDAPKLPENQTSPGES
CCCCCCCCCCCCCCC		48.79UniProtKB CARBOHYD
629PhosphorylationEELWRKLSFRHWPTL
HHHHHHHHHCCCCHH		24.2225554490
641N-linked_GlycosylationPTLFSYYNITLAKRY
CHHHHHCCHHHHHHH		16.73UniProtKB CARBOHYD
677O-linked_GlycosylationRHPQDGRSAWPPPGP
CCCCCCCCCCCCCCC		39.97OGP
822PhosphorylationPGRQRRDSGVGSGLE
CCCCCCCCCCCCCHH		33.3023927012
826PhosphorylationRRDSGVGSGLEAQES
CCCCCCCCCHHHHHH		37.4923927012
833PhosphorylationSGLEAQESWERLSDG
CCHHHHHHHHCCCCC		23.3530266825
838PhosphorylationQESWERLSDGGKAGP
HHHHHCCCCCCCCCC		40.1930266825
842 (in isoform 1)Ubiquitination-56.5521906983
842UbiquitinationERLSDGGKAGPEEPG
HCCCCCCCCCCCCCC		56.552190698
851PhosphorylationGPEEPGDSPPLRHRP
CCCCCCCCCCCCCCC		34.0419664994
865PhosphorylationPRGPPPPSLFGDQPD
CCCCCCCHHHCCCCC		41.9524173317
904PhosphorylationHRAVCGRSRDSPGYD
CCCCCCCCCCCCCCC		26.2325159151
907PhosphorylationVCGRSRDSPGYDFSC
CCCCCCCCCCCCHHH		21.0825159151
910PhosphorylationRSRDSPGYDFSCLVQ
CCCCCCCCCHHHHHH		19.7322617229
913PhosphorylationDSPGYDFSCLVQRVY
CCCCCCHHHHHHHHH		12.0229978859
920PhosphorylationSCLVQRVYQEEGLAA
HHHHHHHHHHCCCEE		16.6427080861
930PhosphorylationEGLAAVCTPALRPPS
CCCEEEECCCCCCCC		12.6626657352
937PhosphorylationTPALRPPSPGPVLSQ
CCCCCCCCCCCCCCC		45.2130175587
943PhosphorylationPSPGPVLSQAPEDEG
CCCCCCCCCCCCCCC		25.2427362937
952PhosphorylationAPEDEGGSPEKGSPS
CCCCCCCCCCCCCCC		40.5220639409
1038PhosphorylationFFSLETHTALSPLQF
EEEEEECCCCCCEEE		36.3929523821
1041PhosphorylationLETHTALSPLQFRGT
EEECCCCCCEEECCC		22.5426074081
1048PhosphorylationSPLQFRGTPGRGSSP
CCEEECCCCCCCCCC		20.5029449344
1051MethylationQFRGTPGRGSSPASP
EECCCCCCCCCCCCC		42.92-
1053PhosphorylationRGTPGRGSSPASPVY
CCCCCCCCCCCCCCC		31.6125137130
1054PhosphorylationGTPGRGSSPASPVYS
CCCCCCCCCCCCCCC		27.5829449344
1057PhosphorylationGRGSSPASPVYSSSD
CCCCCCCCCCCCCCC		20.4825137130
1060PhosphorylationSSPASPVYSSSDTVA
CCCCCCCCCCCCEEE		13.2529449344
1061PhosphorylationSPASPVYSSSDTVAC
CCCCCCCCCCCEEEE		24.4929449344
1062PhosphorylationPASPVYSSSDTVACH
CCCCCCCCCCEEEEE		17.9729449344
1063PhosphorylationASPVYSSSDTVACHL
CCCCCCCCCEEEEEE		31.2129449344
1086MethylationQKPITALKAAAGRLV
CCCHHHHHHHHCCCC		33.25115977579
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
454Kubiquitylation

-
466Kubiquitylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC24B_HUMANSEC24Bphysical
19706601
SRBP1_HUMANSREBF1physical
9242699
SRBP2_HUMANSREBF2physical
9242699
RPTOR_HUMANRPTORphysical
26344197
INSI1_HUMANINSIG1physical
26555173
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 SCAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851 AND SER-907, ANDMASS SPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-243, AND MASSSPECTROMETRY.

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