SEC13_HUMAN - dbPTM
SEC13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SEC13_HUMAN
UniProt AC P55735
Protein Name Protein SEC13 homolog {ECO:0000305}
Gene Name SEC13
Organism Homo sapiens (Human).
Sequence Length 322
Subcellular Localization Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Nucleus, nuclear pore complex . Lysosome membrane . In interphase,
Protein Description Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles.; As a component of the GATOR subcomplex GATOR2, functions within the amino acid-sensing branch of the TORC1 signaling pathway. Indirectly activates mTORC1 and the TORC1 signaling pathway through the inhibition of the GATOR1 subcomplex. [PubMed: 23723238 It is negatively regulated by the upstream amino acid sensors SESN2 and CASTOR1]
Protein Sequence MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQNEQ
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
2Acetylation------MVSVINTVD
------CCEEEECCC		6.6922223895
3Phosphorylation-----MVSVINTVDT
-----CCEEEECCCC		18.9124043423
7Phosphorylation-MVSVINTVDTSHED
-CCEEEECCCCCHHH		14.5024043423
10PhosphorylationSVINTVDTSHEDMIH
EEEECCCCCHHHHHC		27.8724043423
11PhosphorylationVINTVDTSHEDMIHD
EEECCCCCHHHHHCH		22.0320071362
23PhosphorylationIHDAQMDYYGTRLAT
HCHHHHCCCCCEEEE		9.8420071362
24UbiquitinationHDAQMDYYGTRLATC
CHHHHCCCCCEEEEC		14.0421890473
24PhosphorylationHDAQMDYYGTRLATC
CHHHHCCCCCEEEEC		14.0420071362
26PhosphorylationAQMDYYGTRLATCSS
HHHCCCCCEEEECCC		13.3420071362
33PhosphorylationTRLATCSSDRSVKIF
CEEEECCCCCCEEEE		38.91-
35MethylationLATCSSDRSVKIFDV
EEECCCCCCEEEEEE		45.34115493505
38UbiquitinationCSSDRSVKIFDVRNG
CCCCCCEEEEEECCC		38.612189047
38AcetylationCSSDRSVKIFDVRNG
CCCCCCEEEEEECCC		38.6126051181
382-HydroxyisobutyrylationCSSDRSVKIFDVRNG
CCCCCCEEEEEECCC		38.61-
92PhosphorylationIWREENGTWEKSHEH
EEEECCCCEEECHHC		41.87-
161UbiquitinationNAVSWAPAVVPGSLI
CEEEECCCCCCCHHC		13.7521890473
175UbiquitinationIDHPSGQKPNYIKRF
CCCCCCCCCCHHHHH		38.4621890473
180UbiquitinationGQKPNYIKRFASGGC
CCCCCHHHHHHCCCC		30.97-
184PhosphorylationNYIKRFASGGCDNLI
CHHHHHHCCCCHHHH		32.7620873877
187GlutathionylationKRFASGGCDNLIKLW
HHHHCCCCHHHHHHH		3.4122555962
192UbiquitinationGGCDNLIKLWKEEED
CCCHHHHHHHHHHCC		52.00-
195UbiquitinationDNLIKLWKEEEDGQW
HHHHHHHHHHCCCCC		66.73-
207UbiquitinationGQWKEEQKLEAHSDW
CCCCHHHHHHHCCHH		52.12-
212PhosphorylationEQKLEAHSDWVRDVA
HHHHHHCCHHHHHHH		39.97-
223PhosphorylationRDVAWAPSIGLPTST
HHHHCCCCCCCCCHH		22.8821712546
233PhosphorylationLPTSTIASCSQDGRV
CCCHHEEEECCCCCE		15.5121712546
234GlutathionylationPTSTIASCSQDGRVF
CCHHEEEECCCCCEE		2.9022555962
242UbiquitinationSQDGRVFIWTCDDAS
CCCCCEEEEECCCCC		2.4521890473
249PhosphorylationIWTCDDASSNTWSPK
EEECCCCCCCCCCHH		30.9928348404
250PhosphorylationWTCDDASSNTWSPKL
EECCCCCCCCCCHHH		39.7428348404
252PhosphorylationCDDASSNTWSPKLLH
CCCCCCCCCCHHHHH		29.3027251275
254PhosphorylationDASSNTWSPKLLHKF
CCCCCCCCHHHHHHC		15.3229507054
256UbiquitinationSSNTWSPKLLHKFND
CCCCCCHHHHHHCCC		59.1621890473
260UbiquitinationWSPKLLHKFNDVVWH
CCHHHHHHCCCEEEE		45.92-
301PhosphorylationDGQWVCISDVNKGQG
CCEEEEEEEECCCCC		30.3121712546
309PhosphorylationDVNKGQGSVSASVTE
EECCCCCEEEEEECC		12.6625159151
311PhosphorylationNKGQGSVSASVTEGQ
CCCCCEEEEEECCCC		19.2725159151
313PhosphorylationGQGSVSASVTEGQQN
CCCEEEEEECCCCCC		23.2825159151
315PhosphorylationGSVSASVTEGQQNEQ
CEEEEEECCCCCCCC		31.7230108239
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 SEC13_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SEC13_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 SEC13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SC16B_HUMANSEC16Bphysical
16189514
NUP37_HUMANNUP37physical
15146057
NU160_HUMANNUP160physical
15146057
NU133_HUMANNUP133physical
15146057
NU107_HUMANNUP107physical
15146057
NUP85_HUMANNUP85physical
15146057
SC31A_HUMANSEC31Aphysical
15146057
NU145_YEASTNUP145physical
18160040
SEC13_HUMANSEC13physical
18160040
STAM2_HUMANSTAM2physical
19054391
RPAB1_HUMANPOLR2Ephysical
22863883
PRP19_HUMANPRPF19physical
22863883
PSB1_HUMANPSMB1physical
22863883
TRAF5_HUMANTRAF5physical
25416956
SC16B_HUMANSEC16Bphysical
25416956
BCR_HUMANBCRphysical
26186194
NU133_HUMANNUP133physical
26186194
SPDLY_HUMANSPDL1physical
26186194
NUP98_HUMANNUP98physical
26186194
SEH1_HUMANSEH1Lphysical
26186194
NU160_HUMANNUP160physical
26186194
SC31A_HUMANSEC31Aphysical
26186194
MIO_HUMANMIOSphysical
26186194
NUP85_HUMANNUP85physical
26186194
PR38A_HUMANPRPF38Aphysical
26186194
NU107_HUMANNUP107physical
26186194
WDR59_HUMANWDR59physical
26186194
WDR24_HUMANWDR24physical
26186194
STX7_HUMANSTX7physical
26186194
ACY1_HUMANACY1physical
26186194
NUP43_HUMANNUP43physical
26186194
NUP37_HUMANNUP37physical
26186194
MED4_HUMANMED4physical
26186194
TFG_HUMANTFGphysical
26186194
QRIC1_HUMANQRICH1physical
26186194
SESN2_HUMANSESN2physical
26186194
SC24B_HUMANSEC24Bphysical
26344197
WDR24_HUMANWDR24physical
28514442
MIO_HUMANMIOSphysical
28514442
PPWD1_HUMANPPWD1physical
28514442
SPDLY_HUMANSPDL1physical
28514442
SESN2_HUMANSESN2physical
28514442
BCR_HUMANBCRphysical
28514442
NUP98_HUMANNUP98physical
28514442
NUP85_HUMANNUP85physical
28514442
PR38A_HUMANPRPF38Aphysical
28514442
ZBTB5_HUMANZBTB5physical
28514442
NU107_HUMANNUP107physical
28514442
NU160_HUMANNUP160physical
28514442
STX7_HUMANSTX7physical
28514442
ACY1_HUMANACY1physical
28514442
NU133_HUMANNUP133physical
28514442
NUP37_HUMANNUP37physical
28514442
CCD94_HUMANCCDC94physical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
SC16A_HUMANSEC16Aphysical
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 SEC13_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-313, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory