SERC1_HUMAN - dbPTM
SERC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERC1_HUMAN
UniProt AC Q9NRX5
Protein Name Serine incorporator 1
Gene Name SERINC1
Organism Homo sapiens (Human).
Sequence Length 453
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Enhances the incorporation of serine into phosphatidylserine and sphingolipids..
Protein Sequence MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAVHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAIVLFFVYYTHPASCSENKAFISVNMLLCVGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGYNTTSTVPKEGQSVQWWHAQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGARSDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQWTAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD
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
2Myristoylation------MGSVLGLCS
------CCCHHHHHH
26.8524223779
2N-myristoyl glycine------MGSVLGLCS
------CCCHHHHHH
26.85-
31PhosphorylationLLCRCCPSGNNSTVT
EEEEECCCCCHHHHH
39.99-
35PhosphorylationCCPSGNNSTVTRLIY
ECCCCCHHHHHHHHH
28.40-
36PhosphorylationCPSGNNSTVTRLIYA
CCCCCHHHHHHHHHH
28.20-
38PhosphorylationSGNNSTVTRLIYALF
CCCHHHHHHHHHHHH
21.61-
81S-palmitoylationNEKGVVPCNILVGYK
CCCCCCCCCHHCCHH
3.1429575903
105PhosphorylationAMFYLLLSLLMIKVK
HHHHHHHHHHHHHHC
21.3026267517
298N-linked_GlycosylationLLSIIGYNTTSTVPK
HHHHHCEECCCCCCC
31.5019159218
343UbiquitinationSNNSQVNKLTLTSDE
CCCCCCCEEEECCCC
43.9523000965
345PhosphorylationNSQVNKLTLTSDEST
CCCCCEEEECCCCCE
29.6025850435
347PhosphorylationQVNKLTLTSDESTLI
CCCEEEECCCCCEEE
28.9730266825
348PhosphorylationVNKLTLTSDESTLIE
CCEEEECCCCCEEEE
42.3630266825
351PhosphorylationLTLTSDESTLIEDGG
EEECCCCCEEEECCC
33.2430266825
352PhosphorylationTLTSDESTLIEDGGA
EECCCCCEEEECCCC
29.7030266825
361PhosphorylationIEDGGARSDGSLEDG
EECCCCCCCCCCCCC
45.8722167270
364PhosphorylationGGARSDGSLEDGDDV
CCCCCCCCCCCCCCC
33.3129255136
410PhosphorylationTLTNWYRYEPSREMK
HHHCHHHCCCCHHHH
19.2518669648
413PhosphorylationNWYRYEPSREMKSQW
CHHHCCCCHHHHHCC
29.0018669648
418PhosphorylationEPSREMKSQWTAVWV
CCCHHHHHCCEEEEE
29.6420068231
421PhosphorylationREMKSQWTAVWVKIS
HHHHHCCEEEEEEEC
12.0520068231

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 SERC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERC1_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 SERC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMCO1_HUMANTMCO1physical
22939629
ZMY10_HUMANZMYND10physical
21988832
NDUV3_HUMANNDUFV3physical
28514442
LEG3_HUMANLGALS3physical
28514442
GBB2_HUMANGNB2physical
28514442
GPHRA_HUMANGPR89Bphysical
28514442
GPHRB_HUMANGPR89Bphysical
28514442
AAAT_HUMANSLC1A5physical
28514442
METL9_HUMANMETTL9physical
27173435

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 SERC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
N-linked Glycosylation
ReferencePubMed
"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-298, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; THR-352; SER-361;SER-364; TYR-410 AND SER-413, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.

TOP