SNCAP_HUMAN - dbPTM
SNCAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNCAP_HUMAN
UniProt AC Q9Y6H5
Protein Name Synphilin-1
Gene Name SNCAIP
Organism Homo sapiens (Human).
Sequence Length 919
Subcellular Localization Cytoplasm . Detected in cytoplasmic inclusion bodies, together with SNCA.
Protein Description Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1..
Protein Sequence MEAPEYLDLDEIDFSDDISYSVTSLKTIPELCRRCDTQNEDRSVSSSSWNCGISTLITNTQKPTGIADVYSKFRPVKRVSPLKHQPETLENNESDDQKNQKVVEYQKGGESDLGPQPQELGPGDGVGGPPGKSSEPSTSLGELEHYDLDMDEILDVPYIKSSQQLASFTKVTSEKRILGLCTTINGLSGKACSTGSSESSSSNMAPFCVLSPVKSPHLRKASAVIHDQHKLSTEETEISPPLVKCGSAYEPENQSKDFLNKTFSDPHGRKVEKTTPDCQLRAFHLQSSAAESKPEEQVSGLNRTSSQGPEERSEYLKKVKSILNIVKEGQISLLPHLAADNLDKIHDENGNNLLHIAASQGHAECLQHLTSLMGEDCLNERNTEKLTPAGLAIKNGQLECVRWMVSETEAIAELSCSKDFPSLIHYAGCYGQEKILLWLLQFMQEQGISLDEVDQDGNSAVHVASQHGYLGCIQTLVEYGANVTMQNHAGEKPSQSAERQGHTLCSRYLVVVETCMSLASQVVKLTKQLKEQTVERVTLQNQLQQFLEAQKSEGKSLPSSPSSPSSPASRKSQWKSPDADDDSVAKSKPGVQEGIQVLGSLSASSRARPKAKDEDSDKILRQLLGKEISENVCTQEKLSLEFQDAQASSRNSKKIPLEKRELKLARLRQLMQRSLSESDTDSNNSEDPKTTPVRKADRPRPQPIVESVESMDSAESLHLMIKKHTLASGGRRFPFSIKASKSLDGHSPSPTSESSEPDLESQYPGSGSIPPNQPSGDPQQPSPDSTAAQKVATSPKSALKSPSSKRRTSQNLKLRVTFEEPVVQMEQPSLELNGEKDKDKGRTLQRTSTSNESGDQLKRPFGAFRSIMETLSGNQNNNNNYQAANQLKTSTLPLTSLGRKTDAKGNPASSASKGKNKAA
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
71PhosphorylationTGIADVYSKFRPVKR
CCCHHHHHHCCCCCC		25.7625332170
80PhosphorylationFRPVKRVSPLKHQPE
CCCCCCCCCCCCCCC		28.6624719451
167PhosphorylationKSSQQLASFTKVTSE
CCHHHHHHHEECCCC		41.8824719451
188PhosphorylationCTTINGLSGKACSTG
HHEECCCCCCCCCCC		39.3830631047
211PhosphorylationMAPFCVLSPVKSPHL
CCCEEEEECCCCHHH		13.7824719451
215PhosphorylationCVLSPVKSPHLRKAS
EEEECCCCHHHHHHH		20.1316365047
236PhosphorylationHKLSTEETEISPPLV
CCCCCCCCCCCCCCC		32.1826852163
239PhosphorylationSTEETEISPPLVKCG
CCCCCCCCCCCCCCC		17.7721815630
261UbiquitinationQSKDFLNKTFSDPHG
CCHHHHHHHCCCCCC		53.762189047
261UbiquitinationQSKDFLNKTFSDPHG
CCHHHHHHHCCCCCC		53.7621890473
261UbiquitinationQSKDFLNKTFSDPHG
CCHHHHHHHCCCCCC		53.7621890473
299PhosphorylationSKPEEQVSGLNRTSS
CCCHHHCCCCCCCCC		36.9426270265
304PhosphorylationQVSGLNRTSSQGPEE
HCCCCCCCCCCCHHH		31.49-
308UbiquitinationLNRTSSQGPEERSEY
CCCCCCCCHHHHHHH		33.2721890473
308UbiquitinationLNRTSSQGPEERSEY
CCCCCCCCHHHHHHH		33.2721890473
308 (in isoform 3)Ubiquitination-33.27-
308UbiquitinationLNRTSSQGPEERSEY
CCCCCCCCHHHHHHH		33.2721890473
308UbiquitinationLNRTSSQGPEERSEY
CCCCCCCCHHHHHHH		33.2721890473
321PhosphorylationEYLKKVKSILNIVKE
HHHHHHHHHHHHHHH		34.9823312004
387PhosphorylationERNTEKLTPAGLAIK
CCCCCCCCCCEEEEE		23.3518187866
533PhosphorylationTKQLKEQTVERVTLQ
HHHHHHHHHHHHHHH		25.98-
552PhosphorylationQFLEAQKSEGKSLPS
HHHHHHHHCCCCCCC		39.2322468782
556PhosphorylationAQKSEGKSLPSSPSS
HHHHCCCCCCCCCCC		57.2627732954
559PhosphorylationSEGKSLPSSPSSPSS
HCCCCCCCCCCCCCC		61.2427732954
560PhosphorylationEGKSLPSSPSSPSSP
CCCCCCCCCCCCCCC		27.1927732954
562PhosphorylationKSLPSSPSSPSSPAS
CCCCCCCCCCCCCCC		57.7527732954
563PhosphorylationSLPSSPSSPSSPASR
CCCCCCCCCCCCCCC		31.9927732954
565PhosphorylationPSSPSSPSSPASRKS
CCCCCCCCCCCCCHH		51.4027732954
566PhosphorylationSSPSSPSSPASRKSQ
CCCCCCCCCCCCHHH		28.0627732954
569PhosphorylationSSPSSPASRKSQWKS
CCCCCCCCCHHHCCC		43.5627732954
584 (in isoform 6)Phosphorylation-11.35-
648PhosphorylationEFQDAQASSRNSKKI
HHHHHHHHHCCCCCC		20.1129457462
649O-linked_GlycosylationFQDAQASSRNSKKIP
HHHHHHHHCCCCCCC		38.2030379171
674PhosphorylationLRQLMQRSLSESDTD
HHHHHHHHHCCCCCC		21.2523403867
676PhosphorylationQLMQRSLSESDTDSN
HHHHHHHCCCCCCCC		35.9824719451
678PhosphorylationMQRSLSESDTDSNNS
HHHHHCCCCCCCCCC		42.2923403867
680PhosphorylationRSLSESDTDSNNSED
HHHCCCCCCCCCCCC		51.0823403867
725PhosphorylationHLMIKKHTLASGGRR
HHHHHHCCCCCCCCC		32.6624719451
728PhosphorylationIKKHTLASGGRRFPF
HHHCCCCCCCCCCCC		44.9124719451
736PhosphorylationGGRRFPFSIKASKSL
CCCCCCCEEEECCCC		24.3424719451
742PhosphorylationFSIKASKSLDGHSPS
CEEEECCCCCCCCCC		29.24-
747PhosphorylationSKSLDGHSPSPTSES
CCCCCCCCCCCCCCC		32.38-
754PhosphorylationSPSPTSESSEPDLES
CCCCCCCCCCCCHHH		39.51-
755PhosphorylationPSPTSESSEPDLESQ
CCCCCCCCCCCHHHC		49.44-
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
556SPhosphorylationKinaseGSK3BP49841
PSP
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:14506261
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:11590439
-KUbiquitinationE3 ubiquitin ligaseRNF19AQ9NV58
PMID:12750386
-KUbiquitinationE3 ubiquitin ligaseSIAH2O43255
PMID:17982729
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNCAP_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 SNCAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYUA_HUMANSNCAphysical
12044636
GET4_HUMANGET4physical
16169070
SH2D3_HUMANSH2D3Cphysical
16169070
PTN_HUMANPTNphysical
16169070
SYUA_HUMANSNCAphysical
11331421
SYUA_HUMANSNCAphysical
10319874
PRKN_HUMANPARK2physical
11590439
SNCAP_HUMANSNCAIPphysical
19762560
GSK3B_HUMANGSK3Bphysical
16174773
SYUA_HUMANSNCAphysical
15944382
PRKN_HUMANPARK2physical
15944382
SIAH1_HUMANSIAH1physical
15064394
YPT6_YEASTYPT6genetic
20890676
RGP1_YEASTRGP1genetic
20890676
RIC1_YEASTRIC1genetic
20890676
VPS52_YEASTVPS52genetic
20890676
TLG2_YEASTTLG2genetic
20890676
SIAH1_HUMANSIAH1physical
14506261
HERP1_HUMANHERPUD1physical
20604806
PRKN_HUMANPARK2physical
20089136
PRS6B_HUMANPSMC4physical
17327361
ARI1_HUMANARIH1physical
21590270
PRKN_HUMANPARK2physical
21590270
SYUA_HUMANSNCAphysical
15894486
PRKN_HUMANPARK2physical
15894486
PINK1_HUMANPINK1physical
15894486
SNCAP_HUMANSNCAIPphysical
15894486
CSK21_HUMANCSNK2A1physical
14645218
SYUA_HUMANSNCAphysical
14645218
PIN1_HUMANPIN1physical
16365047
SYUA_HUMANSNCAphysical
16365047
PPHLN_MOUSEPphln1physical
19730898
KALRN_HUMANKALRNphysical
23284848
PP1A_HUMANPPP1CAphysical
24902662
PP1G_HUMANPPP1CCphysical
24902662
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
168600Parkinson disease (PARK)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNCAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-387, AND MASSSPECTROMETRY.

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