NICA_HUMAN - dbPTM
NICA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NICA_HUMAN
UniProt AC Q92542
Protein Name Nicastrin
Gene Name NCSTN
Organism Homo sapiens (Human).
Sequence Length 709
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). [PubMed: 10993067]
Protein Sequence MATAGGGSGADPGSRGLLRLLSFCVLLAGLCRGNSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAGLAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTFSINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVDSFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQPLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFVTDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQDLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLYEYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARIFLIASKELELITLTVGFGILIFSLIVTYCINAKADVLFIAPREPGAVSY
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
45N-linked_GlycosylationRKIYIPLNKTAPCVR
EEEEEECCCCCHHHH
33.9930598546
55N-linked_GlycosylationAPCVRLLNATHQIGC
CHHHHHHCCCCCCCC
47.5930598546
101UbiquitinationYMVLLESKHFTRDLM
EEEEEECCCHHHHHH
33.10-
1102-HydroxyisobutyrylationFTRDLMEKLKGRTSR
HHHHHHHHHCCCCCC
41.35-
110AcetylationFTRDLMEKLKGRTSR
HHHHHHHHHCCCCCC
41.3519828433
110UbiquitinationFTRDLMEKLKGRTSR
HHHHHHHHHCCCCCC
41.35-
112AcetylationRDLMEKLKGRTSRIA
HHHHHHHCCCCCCCE
58.3719828441
127UbiquitinationGLAVSLTKPSPASGF
EEEEECCCCCCCCCC
49.11-
187N-linked_GlycosylationIFLLEDENETKVIKQ
EEEECCCCCHHHHHH
74.6530598546
200N-linked_GlycosylationKQCYQDHNLSQNGSA
HHHHHHCCCCCCCCC
50.07UniProtKB CARBOHYD
204N-linked_GlycosylationQDHNLSQNGSAPTFP
HHCCCCCCCCCCCHH
42.90UniProtKB CARBOHYD
264N-linked_GlycosylationWSMLKPINTTGTLKP
HHHCCCCCCCCCCCC
39.8630598546
319PhosphorylationLQKAPDVTTLPRNVM
HHHCCCCCCCCCCEE
29.9622798277
320PhosphorylationQKAPDVTTLPRNVMF
HHCCCCCCCCCCEEE
34.3122798277
331 (in isoform 2)Ubiquitination-37.0321906983
349UbiquitinationRMVYDMEKGKFPVQL
EEEEECCCCCCCEEE
61.84-
3492-HydroxyisobutyrylationRMVYDMEKGKFPVQL
EEEEECCCCCCCEEE
61.84-
349AcetylationRMVYDMEKGKFPVQL
EEEEECCCCCCCEEE
61.8412655271
351 (in isoform 1)Ubiquitination-58.5221906983
351UbiquitinationVYDMEKGKFPVQLEN
EEECCCCCCCEEECC
58.5221906983
383 (in isoform 2)Ubiquitination-12.0221906983
387N-linked_GlycosylationTDPVSQKNESVRNQV
CCCCHHCCHHHHHHH
38.8630598546
400PhosphorylationQVEDLLATLEKSGAG
HHHHHHHHHHHCCCC
35.1024719451
403UbiquitinationDLLATLEKSGAGVPA
HHHHHHHHCCCCCCE
58.252190698
403 (in isoform 1)Ubiquitination-58.2521906983
417N-linked_GlycosylationAVILRRPNQSQPLPP
EEEEECCCCCCCCCH
52.93UniProtKB CARBOHYD
425PhosphorylationQSQPLPPSSLQRFLR
CCCCCCHHHHHHHHH
41.56-
426PhosphorylationSQPLPPSSLQRFLRA
CCCCCHHHHHHHHHH
34.00-
434MethylationLQRFLRARNISGVVL
HHHHHHHCCCCCEEE
34.2812019821
435N-linked_GlycosylationQRFLRARNISGVVLA
HHHHHHCCCCCEEEE
31.6230598546
437PhosphorylationFLRARNISGVVLADH
HHHHCCCCCEEEECC
29.1422590650
464N-linked_GlycosylationYDTAENINVSYPEWL
HHHHHHCCCCCCCCC
28.4130598546
506N-linked_GlycosylationYELAGGTNFSDTVQA
HHHHCCCCCHHHCCC
37.3930598546
530N-linked_GlycosylationYGFLIKANNSWFQSI
HHHHHHHCCHHHHHH
37.7630598546
536PhosphorylationANNSWFQSILRQDLR
HCCHHHHHHHHHHHH
17.7024719451
562N-linked_GlycosylationIAVSSPTNTTYVVQY
EEEECCCCCHHHHHH
33.5330598546
573N-linked_GlycosylationVVQYALANLTGTVVN
HHHHHHHHCCCCEEE
38.7030598546
580N-linked_GlycosylationNLTGTVVNLTREQCQ
HCCCCEEECCHHHCC
31.2130630874
612N-linked_GlycosylationVQGPLHSNETDRLPR
ECCCCCCCCCCCHHH
45.5019349973
612N-linked_GlycosylationVQGPLHSNETDRLPR
ECCCCCCCCCCCHHH
45.5019349973
632PhosphorylationARLARALSPAFELSQ
HHHHHHHCCHHHHHH
17.13-
638PhosphorylationLSPAFELSQWSSTEY
HCCHHHHHHCCCCCC
23.54-
647PhosphorylationWSSTEYSTWTESRWK
CCCCCCCCCCHHHHH
35.19-
649PhosphorylationSTEYSTWTESRWKDI
CCCCCCCCHHHHHHH
24.95-
672PhosphorylationSKELELITLTVGFGI
CCCCHHHHHHHHHHH
29.06-
674PhosphorylationELELITLTVGFGILI
CCHHHHHHHHHHHHH
15.21-
689S-palmitoylationFSLIVTYCINAKADV
HHHHHHHHHHCCCCE
1.0919028695
708PhosphorylationPREPGAVSY------
CCCCCCCCC------
25.2925159151
708O-linked_GlycosylationPREPGAVSY------
CCCCCCCCC------
25.2922503002

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
437SPhosphorylationKinaseSGK1O00141
PSP
-KUbiquitinationE3 ubiquitin ligaseSYVN1Q86TM6
PMID:19725872

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NICA_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 NICA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APH1A_HUMANAPH1Aphysical
15257293
PSN1_HUMANPSEN1physical
15257293
PEN2_HUMANPSENENphysical
14572442
APH1A_HUMANAPH1Aphysical
14572442
PSN1_HUMANPSEN1physical
14572442
APH1A_HUMANAPH1Aphysical
12471034
PSN1_HUMANPSEN1physical
12471034
APH1A_HUMANAPH1Aphysical
12297508
PSN1_HUMANPSEN1physical
12297508
PSN2_HUMANPSEN2physical
12297508
PSN1_HUMANPSEN1physical
10993067
PSN2_HUMANPSEN2physical
10993067
A4_HUMANAPPphysical
10993067
BACE1_HUMANBACE1physical
12054507
RS14_HUMANRPS14physical
22939629
TR150_HUMANTHRAP3physical
22939629
RAD50_HUMANRAD50physical
22939629
SRS11_HUMANSRSF11physical
22939629
SEPT7_HUMANSEPT7physical
22939629
SEPT2_HUMANSEPT2physical
22939629
SPB1_HUMANFTSJ3physical
22939629
SNUT2_HUMANUSP39physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
RS11_HUMANRPS11physical
22939629
RBM25_HUMANRBM25physical
22939629
PRP6_HUMANPRPF6physical
22939629
SRS10_HUMANSRSF10physical
22939629
RRS1_HUMANRRS1physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
TRI55_HUMANTRIM55physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
PSIP1_HUMANPSIP1physical
22939629
NUMA1_HUMANNUMA1physical
22939629
NOP56_HUMANNOP56physical
22939629
TOP1_HUMANTOP1physical
22939629
SERA_HUMANPHGDHphysical
22939629
SURF4_HUMANSURF4physical
22939629
RCC1_HUMANRCC1physical
22939629
TOP2B_HUMANTOP2Bphysical
22939629
PR40A_HUMANPRPF40Aphysical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SRSF1_HUMANSRSF1physical
22939629
RFC4_HUMANRFC4physical
22939629
SAP18_HUMANSAP18physical
22939629
NOP58_HUMANNOP58physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
U2AF1_HUMANU2AF1physical
22939629
NOP16_HUMANNOP16physical
22939629
S27A2_HUMANSLC27A2physical
22939629
RCC2_HUMANRCC2physical
22939629
SPF27_HUMANBCAS2physical
22939629
NOP2_HUMANNOP2physical
22939629
PCDA2_HUMANPCDHA2physical
22939629
TPBG_HUMANTPBGphysical
22939629
TF3C1_HUMANGTF3C1physical
22939629
S10A9_HUMANS100A9physical
22939629
SMD2_HUMANSNRPD2physical
22939629
SSRP1_HUMANSSRP1physical
22939629
RS7_HUMANRPS7physical
22939629
RED_HUMANIKphysical
22939629
REQU_HUMANDPF2physical
22939629
SMCA5_HUMANSMARCA5physical
22939629
SNF5_HUMANSMARCB1physical
22939629
SNUT1_HUMANSART1physical
22939629
TR112_HUMANTRMT112physical
22939629
WDR18_HUMANWDR18physical
22939629
RL1D1_HUMANRSL1D1physical
22939629
SMU1_HUMANSMU1physical
22939629
ZCH18_HUMANZC3H18physical
22939629
RAB31_HUMANRAB31physical
22939629
SAFB1_HUMANSAFBphysical
22939629
TM14B_HUMANTMEM14Bphysical
22939629
ERLN2_HUMANERLIN2physical
22771797
HNRPF_HUMANHNRNPFphysical
26344197
ALDOA_HUMANALDOAphysical
26496610
ADT2_HUMANSLC25A5physical
26496610
AT1A1_HUMANATP1A1physical
26496610
AT2A2_HUMANATP2A2physical
26496610
ATPA_HUMANATP5A1physical
26496610
BASI_HUMANBSGphysical
26496610
NDUB5_HUMANNDUFB5physical
26496610
GTR1_HUMANSLC2A1physical
26496610
LAT1_HUMANSLC7A5physical
26496610
CMC1_HUMANSLC25A12physical
26496610
PCH2_HUMANTRIP13physical
26496610
TTI1_HUMANTTI1physical
26496610
TOM20_HUMANTOMM20physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
RPP38_HUMANRPP38physical
26496610
SPTC1_HUMANSPTLC1physical
26496610
EBP_HUMANEBPphysical
26496610
YIF1A_HUMANYIF1Aphysical
26496610
MAGD2_HUMANMAGED2physical
26496610
TEST_HUMANPRSS21physical
26496610
MIC60_HUMANIMMTphysical
26496610
ERLN2_HUMANERLIN2physical
26496610
ELL2_HUMANELL2physical
26496610
PNKD_HUMANPNKDphysical
26496610
TECT3_HUMANTCTN3physical
26496610
CRNL1_HUMANCRNKL1physical
26496610
TRM6_HUMANTRMT6physical
26496610
ESYT2_HUMANESYT2physical
26496610
SQOR_HUMANSQRDLphysical
26496610
SRPRB_HUMANSRPRBphysical
26496610
FAKD5_HUMANFASTKD5physical
26496610
F111A_HUMANFAM111Aphysical
26496610
MMS19_HUMANMMS19physical
26496610
WLS_HUMANWLSphysical
26496610
CLP1L_HUMANCLPTM1Lphysical
26496610
MAGT1_HUMANMAGT1physical
26496610
TIM29_HUMANC19orf52physical
26496610
SFXN1_HUMANSFXN1physical
26496610
ACTS_HUMANACTA1physical
28514442
LOX5_HUMANALOX5physical
28514442
MICA1_HUMANMICAL1physical
28514442
RRAS_HUMANRRASphysical
28514442
SRC_HUMANSRCphysical
28514442
PHAG1_HUMANPAG1physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
EEPD1_HUMANEEPD1physical
28514442
PTPRG_HUMANPTPRGphysical
28514442
VASN_HUMANVASNphysical
28514442
AHNK2_HUMANAHNAK2physical
28514442
EPHA2_HUMANEPHA2physical
28514442
YES_HUMANYES1physical
28514442
RAP2A_HUMANRAP2Aphysical
28514442
NCAM1_HUMANNCAM1physical
28514442
APH1A_HUMANAPH1Aphysical
18667537
PSN1_HUMANPSEN1physical
18667537
PEN2_HUMANPSENENphysical
18667537

Drug and Disease Associations
Kegg Disease
H00681 Acne inversa; Hidradenitis supprativa
OMIM Disease
142690Acne inversa, familial, 1 (ACNINV1)
Kegg Drug
D08869 Begacestat (USAN/INN)
D09010 Tarenflurbil (USAN/INN); R-Flurbiprofen
D09377 Semagacestat (USAN/INN)
D09869 Avagacestat (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NICA_HUMAN

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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-612, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-187 AND ASN-387,AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-387.

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