NICA_MOUSE - dbPTM
NICA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NICA_MOUSE
UniProt AC P57716
Protein Name Nicastrin
Gene Name Ncstn
Organism Mus musculus (Mouse).
Sequence Length 708
Subcellular Localization Membrane
Single-pass type I membrane protein . Cytoplasmic vesicle membrane
Single-pass type I membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels..
Protein Sequence MATTRGGSGPDPGSRGLLLLSFSVVLAGLCGGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLKWVLTDGPNPPYMVLLEGKLFTRDVMEKLKGTTSRIAGLAVTLAKPNSTSSFSPSVQCPNDGFGIYSNSYGPEFAHCKKTLWNELGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLGQNGSAPSFPLCAMQLFSHMHAVISTATCMRRSFIQSTFSINPEIVCDPLSDYNVWSMLKPINTSVGLEPDVRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALHKAPDVTTLSRNVMFVFFQGETFDYIGSSRMVYDMENGKFPVRLENIDSFVELGQVALRTSLDLWMHTDPMSQKNESVKNQVEDLLATLEKSGAGVPEVVLRRLAQSQALPPSSLQRFLRARNISGVVLADHSGSFHNRYYQSIYDTAENINVTYPEWQSPEEDLNFVTDTAKALANVATVLARALYELAGGTNFSSSIQADPQTVTRLLYGFLVRANNSWFQSILKHDLRSYLDDRPLQHYIAVSSPTNTTYVVQYALANLTGKATNLTREQCQDPSKVPNESKDLYEYSWVQGPWNSNRTERLPQCVRSTVRLARALSPAFELSQWSSTEYSTWAESRWKDIQARIFLIASKELEFITLIVGFSTLVFSLIVTYCINAKADVLFVAPREPGAVSY
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
3Phosphorylation-----MATTRGGSGP
-----CCCCCCCCCC		18.7424719451
44N-linked_GlycosylationRKIYIPLNKTAPCVR
EEEEEECCCCCHHHH		33.99-
54N-linked_GlycosylationAPCVRLLNATHQIGC
CHHHHHHCCCCCCCC		47.59-
128N-linked_GlycosylationAVTLAKPNSTSSFSP
EEEECCCCCCCCCCC		58.16-
186N-linked_GlycosylationIFLLEDENETKVIKQ
EEEECCCCCHHHHHH		74.6519349973
203N-linked_GlycosylationQDHNLGQNGSAPSFP
HHCCCCCCCCCCCHH		44.59-
240PhosphorylationSFIQSTFSINPEIVC
HHHHHCCCCCCCCEE		22.88-
263N-linked_GlycosylationWSMLKPINTSVGLEP
HHHCCCCCCCCCCCC		34.5219349973
386N-linked_GlycosylationTDPMSQKNESVKNQV
CCCCCHHCHHHHHHH		38.8619349973
434N-linked_GlycosylationQRFLRARNISGVVLA
HHHHHHCCCCCEEEE		31.62-
463N-linked_GlycosylationYDTAENINVTYPEWQ
HHCHHCCCCCCCCCC		31.49-
505N-linked_GlycosylationYELAGGTNFSSSIQA
HHHHCCCCCCCCCCC		37.7719349973
529N-linked_GlycosylationYGFLVRANNSWFQSI
HHHHHHCCCHHHHHH		32.29-
530N-linked_GlycosylationGFLVRANNSWFQSIL
HHHHHCCCHHHHHHH		39.3719349973
561N-linked_GlycosylationIAVSSPTNTTYVVQY
EEEECCCCHHHHHHH		33.5319349973
572N-linked_GlycosylationVVQYALANLTGKATN
HHHHHHHHCCCCHHC		38.70-
579N-linked_GlycosylationNLTGKATNLTREQCQ
HCCCCHHCCCHHHCC		44.25-
593N-linked_GlycosylationQDPSKVPNESKDLYE
CCCCCCCCCCCCCHH		69.98-
611N-linked_GlycosylationVQGPWNSNRTERLPQ
CCCCCCCCHHHCHHH		52.2419349973
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
-KUbiquitinationE3 ubiquitin ligaseSyvn1Q9DBY1
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NICA_MOUSE !!
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 NICA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYVN1_MOUSESyvn1physical
19725872
HERP1_MOUSEHerpud1physical
21600962
PSN1_MOUSEPsen1physical
11943765
ENPL_MOUSEHsp90b1physical
11943765
GRP78_MOUSEHspa5physical
11943765
EEA1_MOUSEEea1physical
11943765
COPD_HUMANARCN1physical
26496610
BASI_HUMANBSGphysical
26496610
CALX_HUMANCANXphysical
26496610
COPA_HUMANCOPAphysical
26496610
VKGC_HUMANGGCXphysical
26496610
LMNB1_HUMANLMNB1physical
26496610
MD2L1_HUMANMAD2L1physical
26496610
NDUB5_HUMANNDUFB5physical
26496610
AAPK1_HUMANPRKAA1physical
26496610
PSN1_HUMANPSEN1physical
26496610
AAAT_HUMANSLC1A5physical
26496610
ELOC_HUMANTCEB1physical
26496610
MBD4_HUMANMBD4physical
26496610
ATPK_HUMANATP5J2physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
CMC2_HUMANSLC25A13physical
26496610
SPTC1_HUMANSPTLC1physical
26496610
OS9_HUMANOS9physical
26496610
ERLEC_HUMANERLEC1physical
26496610
FABD_HUMANMCATphysical
26496610
NOB1_HUMANNOB1physical
26496610
RM02_HUMANMRPL2physical
26496610
NDUAD_HUMANNDUFA13physical
26496610
TRM6_HUMANTRMT6physical
26496610
GNL3L_HUMANGNL3Lphysical
26496610
S35F6_HUMANSLC35F6physical
26496610
RIF1_HUMANRIF1physical
26496610
ASF1B_HUMANASF1Bphysical
26496610
PRR12_HUMANPRR12physical
26496610
DERL1_HUMANDERL1physical
26496610
WLS_HUMANWLSphysical
26496610
K2013_HUMANKIAA2013physical
26496610
MCU_HUMANMCUphysical
26496610
TATD3_HUMANTATDN3physical
26496610
STT3B_HUMANSTT3Bphysical
26496610
TIM23_HUMANTIMM23physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NICA_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186; ASN-263; ASN-386;ASN-505; ASN-530; ASN-561 AND ASN-611, AND MASS SPECTROMETRY.

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