SARAF_HUMAN - dbPTM
SARAF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SARAF_HUMAN
UniProt AC Q96BY9
Protein Name Store-operated calcium entry-associated regulatory factor
Gene Name SARAF
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein . Translocates to the endoplasmic reticulum-plasma membrane (ER-PM) region in a STIM1-dependent manner following cytosolic Ca(2+) elevation.
Isoform 2: Endoplasmic reticulum membra
Protein Description Negative regulator of store-operated Ca(2+) entry (SOCE) involved in protecting cells from Ca(2+) overfilling. In response to cytosolic Ca(2+) elevation after endoplasmic reticulum Ca(2+) refilling, promotes a slow inactivation of STIM (STIM1 or STIM2)-dependent SOCE activity: possibly act by facilitating the deoligomerization of STIM to efficiently turn off ORAI when the endoplasmic reticulum lumen is filled with the appropriate Ca(2+) levels, and thus preventing the overload of the cell with excessive Ca(2+) ions..
Protein Sequence MAAACGPGAAGYCLLLGLHLFLLTAGPALGWNDPDRMLLRDVKALTLHYDRYTTSRRLDPIPQLKCVGGTAGCDSYTPKVIQCQNKGWDGYDVQWECKTDLDIAYKFGKTVVSCEGYESSEDQYVLRGSCGLEYNLDYTELGLQKLKESGKQHGFASFSDYYYKWSSADSCNMSGLITIVVLLGIAFVVYKLFLSDGQYSPPPYSEYPPFSHRYQRFTNSAGPPPPGFKSEFTGPQNTGHGATSGFGSAFTGQQGYENSGPGFWTGLGTGGILGYLFGSNRAATPFSDSWYYPSYPPSYPGTWNRAYSPLHGGSGSYSVCSNSDTKTRTASGYGGTRRR
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
43UbiquitinationRMLLRDVKALTLHYD
HHHHHHHHHHHHHCC		41.8021890473
43UbiquitinationRMLLRDVKALTLHYD
HHHHHHHHHHHHHCC		41.8021890473
49PhosphorylationVKALTLHYDRYTTSR
HHHHHHHCCCCCCCC		12.7729759185
52PhosphorylationLTLHYDRYTTSRRLD
HHHHCCCCCCCCCCC		16.0929759185
65UbiquitinationLDPIPQLKCVGGTAG
CCCCCCCEECCCCCC		22.94-
79UbiquitinationGCDSYTPKVIQCQNK
CCCCCCCCEEEEECC		44.1421890473
86UbiquitinationKVIQCQNKGWDGYDV
CEEEEECCCCCCCCE		35.18-
105PhosphorylationKTDLDIAYKFGKTVV
ECCHHHHHHCCCEEE		13.7420049867
106UbiquitinationTDLDIAYKFGKTVVS
CCHHHHHHCCCEEEE		38.3221890473
106UbiquitinationTDLDIAYKFGKTVVS
CCHHHHHHCCCEEEE		38.3221890473
109UbiquitinationDIAYKFGKTVVSCEG
HHHHHCCCEEEEECC		41.0821890473
110PhosphorylationIAYKFGKTVVSCEGY
HHHHCCCEEEEECCC		26.9020049867
113PhosphorylationKFGKTVVSCEGYESS
HCCCEEEEECCCCCC		11.3420049867
117PhosphorylationTVVSCEGYESSEDQY
EEEEECCCCCCCCEE		7.1420049867
119PhosphorylationVSCEGYESSEDQYVL
EEECCCCCCCCEEEE		30.4620049867
120PhosphorylationSCEGYESSEDQYVLR
EECCCCCCCCEEEEE		33.0020049867
124PhosphorylationYESSEDQYVLRGSCG
CCCCCCEEEEECCCC		17.4920049867
145UbiquitinationYTELGLQKLKESGKQ
HHHHHHHHHHHHCCC		67.5721890473
147UbiquitinationELGLQKLKESGKQHG
HHHHHHHHHHCCCCC		57.79-
151UbiquitinationQKLKESGKQHGFASF
HHHHHHCCCCCCCCH		48.69-
167PhosphorylationDYYYKWSSADSCNMS
HCEEECCCCCCCCHH		34.6719413330
170PhosphorylationYKWSSADSCNMSGLI
EECCCCCCCCHHHHH		13.7019413330
174PhosphorylationSADSCNMSGLITIVV
CCCCCCHHHHHHHHH		19.2224043423
178PhosphorylationCNMSGLITIVVLLGI
CCHHHHHHHHHHHHH		16.8624043423
190PhosphorylationLGIAFVVYKLFLSDG
HHHHHHHHHHHCCCC		9.1819413330
220PhosphorylationRYQRFTNSAGPPPPG
HHHHHCCCCCCCCCC		31.3928555341
265PhosphorylationNSGPGFWTGLGTGGI
CCCCCCCCCCCCCHH		21.92-
307PhosphorylationPGTWNRAYSPLHGGS
CCCCCCCCCCCCCCC		13.9521815630
308PhosphorylationGTWNRAYSPLHGGSG
CCCCCCCCCCCCCCC		21.7221815630
314PhosphorylationYSPLHGGSGSYSVCS
CCCCCCCCCCEEEEC		29.2022199227
316PhosphorylationPLHGGSGSYSVCSNS
CCCCCCCCEEEECCC		18.8722199227
317PhosphorylationLHGGSGSYSVCSNSD
CCCCCCCEEEECCCC		14.5122199227
318PhosphorylationHGGSGSYSVCSNSDT
CCCCCCEEEECCCCC		20.5327794612
321PhosphorylationSGSYSVCSNSDTKTR
CCCEEEECCCCCCCE		36.8922199227
323PhosphorylationSYSVCSNSDTKTRTA
CEEEECCCCCCCEEC		30.2921815630
325PhosphorylationSVCSNSDTKTRTASG
EEECCCCCCCEECCC		33.8521815630
326UbiquitinationVCSNSDTKTRTASGY
EECCCCCCCEECCCC		40.7921890473
327PhosphorylationCSNSDTKTRTASGYG
ECCCCCCCEECCCCC		35.0323532336
331PhosphorylationDTKTRTASGYGGTRR
CCCCEECCCCCCCCC		31.7528857561
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 SARAF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SARAF_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 SARAF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SE1L1_HUMANSEL1Lphysical
18502753
SYVN1_HUMANSYVN1physical
18502753
AMFR_HUMANAMFRphysical
18502753
OS9_HUMANOS9physical
18502753
ITCH_HUMANITCHphysical
28514442
WWP1_HUMANWWP1physical
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 SARAF_HUMAN

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Related Literatures of Post-Translational Modification

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