SCAP_SCHPO - dbPTM
SCAP_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCAP_SCHPO
UniProt AC O43043
Protein Name Sterol regulatory element-binding protein cleavage-activating protein
Gene Name scp1 {ECO:0000312|EMBL:CAA17795.1}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1086
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description Escort protein required for sre1 processing at low sterol as well as oxygen levels. May regulate export of the scp1/sre1 complex from the ER at low sterol or oxygen levels. 4-methyl sterols bound to scp1 may mask an ER-export signal in scp1 leading to retention of the complex in the ER. Release of 4-methyl sterols may trigger a conformational change in the SSC domain of scp1 unmasking the ER export signal leading to recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of sre1 in the Golgi, release of the transcription factor fragment of sre1 from the membrane, its import into the nucleus and up-regulation of genes required for ergosterol biosynthesis as well as anaerobic growth..
Protein Sequence MRIFTLGKGRISRGYARQVNPSLFAKYSYCIANNPWYFILVFTLLSITGIYSSLVAYQQSLYDQSLARWSAWYAESINAEANVITKQLYLLGTNTSVFSEDYLSNAYRWETSFHQYLAEYGYPCIRDEKSCVTISPIPKYYGKVDPVAQYSYTKGLPENEREVNKLRNDTIAEGFDSLSAFVITYFLKPEQVDTFHVVLKKFISETPNLYASLLDTSPTTVVARIPDLTVIYRWYLWVGFGVGLFAYLYLSLVRLHDIRAKFGLTATIFIQSGTAYFSTCSLLYFFERTGPICPWPMAYYIIIFMDIENSFRLLRAVIASPQTKRVPSRIMEGFSSTIIASFSSLLKKLLTLFVLSFFVYPLVQEFCLFLACSFVVSFLLHGSFFLAVLSVDIRRLELQDFLDSNSSNRNSKWWVPYLEYVRFMWSPWIIDNLGTVSFHMYVIYLQLQSSTDINGSWRLASPNIRFLITLYHRLGRILRERKLFPLITTGWFGDPTFLEALKEKTMAENLVIALYRPVILDTVNRRDYTNVYNSFHDRRVWRWSTFFSILFAIDFAVGLLVKALLRGWSDHDELSTDTTLHEEKFRIEPVPVHHQLDILKIAVSENYKTFASVGLDRCLVVWDLRQWCTKLVLSKEQMPRTLKAIALDPQGNYVSLFSKDTLFILNVESPCLMLQHSYHCKPNSKLNVFWMPGTHKDDEWKNFELVVVESSGEIQVFSLTIEIEGADIALVEKFQLSSPIIKSISIVSPTANRIACLTESGEVTVYSKKGPVWSPKILSQNKNYLTETKKDIYGIAMADILFLARDSGVDMIDLKNDELLHSFTLPPIKVNTFSVGVSNSRFVNGQFRVSSISFCFTHAVTEKVLYYYYGNECNESYIILNKWDQQPNLVDVHDPDNSLACLTFDELQENIHEVEDASECVMSSDGLYIFGMRRKSSSGICPTADEKNEDNGFTLRNRKLRTGHYNWTSYVPLLDSYMQDMEHKKNTHSGGETQVWEVWMYSQSEKKHRCKSLKMYNSLIIADPGPSLAVSDRCVAIVLGNYVALVGYGSEIFRDFYQIRNSDEMDRILRRKRKNLQRKRSGTIGC
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
94N-linked_GlycosylationQLYLLGTNTSVFSED
EEHHHCCCCCCCCHH
28.67-
168N-linked_GlycosylationREVNKLRNDTIAEGF
HHHHHHCCCHHHHCH
62.30-
454N-linked_GlycosylationLQSSTDINGSWRLAS
CCCCCCCCCCEEECC
41.05-

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_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SREBP_SCHPOsre1physical
15797383
SREBP_SCHPOsre1genetic
22086920
RYH1_SCHPOryh1genetic
22681890
SFT1_SCHPOsft1genetic
22681890
VTS1_SCHPOSPBC13E7.03cgenetic
22681890
NCPR_SCHPOccr1genetic
22681890
SCAP_SCHPOscp1physical
26771498

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

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Related Literatures of Post-Translational Modification

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