SNAG_HUMAN - dbPTM
SNAG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNAG_HUMAN
UniProt AC Q99747
Protein Name Gamma-soluble NSF attachment protein
Gene Name NAPG
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Membrane
Peripheral membrane protein.
Protein Description Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus..
Protein Sequence MAAQKINEGLEHLAKAEKYLKTGFLKWKPDYDSAASEYGKAAVAFKNAKQFEQAKDACLREAVAHENNRALFHAAKAYEQAGMMLKEMQKLPEAVQLIEKASMMYLENGTPDTAAMALERAGKLIENVDPEKAVQLYQQTANVFENEERLRQAVELLGKASRLLVRGRRFDEAALSIQKEKNIYKEIENYPTCYKKTIAQVLVHLHRNDYVAAERCVRESYSIPGFNGSEDCAALEQLLEGYDQQDQDQVSDVCNSPLFKYMDNDYAKLGLSLVVPGGGIKKKSPATPQAKPDGVTATAADEEEDEYSGGLC
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
5Acetylation---MAAQKINEGLEH
---CCHHHHHHHHHH		42.6525953088
19PhosphorylationHLAKAEKYLKTGFLK
HHHHHHHHHHHCCCC		12.6330576142
28UbiquitinationKTGFLKWKPDYDSAA
HHCCCCCCCCHHHHH		26.82-
28AcetylationKTGFLKWKPDYDSAA
HHCCCCCCCCHHHHH		26.8226051181
31PhosphorylationFLKWKPDYDSAASEY
CCCCCCCHHHHHHHH		21.9628796482
33PhosphorylationKWKPDYDSAASEYGK
CCCCCHHHHHHHHHH		21.3628796482
36PhosphorylationPDYDSAASEYGKAAV
CCHHHHHHHHHHHHH		30.9428796482
38PhosphorylationYDSAASEYGKAAVAF
HHHHHHHHHHHHHHH		22.7928796482
46AcetylationGKAAVAFKNAKQFEQ
HHHHHHHHCHHHHHH		46.3826051181
49AcetylationAVAFKNAKQFEQAKD
HHHHHCHHHHHHHHH		65.9825953088
55UbiquitinationAKQFEQAKDACLREA
HHHHHHHHHHHHHHH		45.62-
78PhosphorylationLFHAAKAYEQAGMML
HHHHHHHHHHHCHHH		14.1022210691
102PhosphorylationVQLIEKASMMYLENG
HHHHHHHHHHHHHCC		18.3625332170
105PhosphorylationIEKASMMYLENGTPD
HHHHHHHHHHCCCHH		11.3922817900
110PhosphorylationMMYLENGTPDTAAMA
HHHHHCCCHHHHHHH		29.5828348404
113PhosphorylationLENGTPDTAAMALER
HHCCCHHHHHHHHHH		19.95-
123MalonylationMALERAGKLIENVDP
HHHHHHHHHHHCCCH		45.3526320211
123UbiquitinationMALERAGKLIENVDP
HHHHHHHHHHHCCCH		45.35-
123AcetylationMALERAGKLIENVDP
HHHHHHHHHHHCCCH		45.3525953088
132UbiquitinationIENVDPEKAVQLYQQ
HHCCCHHHHHHHHHH		60.28-
137PhosphorylationPEKAVQLYQQTANVF
HHHHHHHHHHHHCHH		4.9827642862
184PhosphorylationIQKEKNIYKEIENYP
HHHHHHHHHHHHCCC		16.3827642862
185UbiquitinationQKEKNIYKEIENYPT
HHHHHHHHHHHCCCH		48.71-
190PhosphorylationIYKEIENYPTCYKKT
HHHHHHCCCHHHHHH		6.2722817900
195AcetylationENYPTCYKKTIAQVL
HCCCHHHHHHHHHHH		45.6627452117
1952-HydroxyisobutyrylationENYPTCYKKTIAQVL
HCCCHHHHHHHHHHH		45.66-
210PhosphorylationVHLHRNDYVAAERCV
HHHHCCCHHHHHHHH		8.7828796482
266PhosphorylationFKYMDNDYAKLGLSL
HHHCCCCHHHHCCEE		16.3427642862
272PhosphorylationDYAKLGLSLVVPGGG
CHHHHCCEEEECCCC		19.8124719451
284PhosphorylationGGGIKKKSPATPQAK
CCCCCCCCCCCCCCC		28.7525159151
287PhosphorylationIKKKSPATPQAKPDG
CCCCCCCCCCCCCCC		21.2225159151
296PhosphorylationQAKPDGVTATAADEE
CCCCCCEEEEECCCC		24.6630108239
298PhosphorylationKPDGVTATAADEEED
CCCCEEEEECCCCCC		17.0130576142
307PhosphorylationADEEEDEYSGGLC--
CCCCCCCCCCCCC--		25.5721082442
308PhosphorylationDEEEDEYSGGLC---
CCCCCCCCCCCC---		25.0828796482
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 SNAG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNAG_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 SNAG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP5_HUMANRAB11FIP5physical
11278501
RFIP5_MOUSERab11fip5physical
11278501
TBG1_HUMANTUBG1physical
11278501
AKA11_HUMANAKAP11physical
26186194
SNAA_HUMANNAPAphysical
26186194
SCFD2_HUMANSCFD2physical
26186194
KAPCB_HUMANPRKACBphysical
26186194
KAP1_HUMANPRKAR1Bphysical
26186194
VAMP4_HUMANVAMP4physical
26186194
STX8_HUMANSTX8physical
26186194
NBAS_HUMANNBASphysical
26186194
STX8_HUMANSTX8physical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
SCFD2_HUMANSCFD2physical
28514442
NBAS_HUMANNBASphysical
28514442
UFSP2_HUMANUFSP2physical
28514442
SNAA_HUMANNAPAphysical
28514442
KAPCB_HUMANPRKACBphysical
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 SNAG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-307, AND MASSSPECTROMETRY.

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