COPG_YEAST - dbPTM
COPG_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPG_YEAST
UniProt AC P32074
Protein Name Coatomer subunit gamma
Gene Name SEC21
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 935
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Endosome. The coatomer is cytoplasmic or polymerized on the cytoplas
Protein Description The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins..
Protein Sequence MSAHTYKKFENSTSGDLPDKMTIYQDCMNTFNESPVNSKRCRLLISRLLRLLAQGETFPQNEATALFFSISKLFQHQNDPLRQAVYLAIKELSGISEDVLMATSSIMKDVQNGSDLIKPDAIRSLTYVLDESTAFSAERLLKSAVVSRHPSISSAALCTSYHLLPISEVTIRRFTNETQEAVLDLKQFPNQHGNSEYYPNSTYISQYHALGLLYQLKKTDKMALLKLVRHFSENNSMKNQLAKVELVKIVNDLIYRDPQLFSQFRPLLSDWLSNKFESVQLETAKLITSFATRNSRLVAPELYAAAISALQSLLTVPRVSSRFAALRILNRISMVSPEKIVVCNPELESLINDSNRNISTYAITTLLKTGTSKNISSLISTITNFIHDVSDDFKIIIIDAVRTLSLNFPQEWKSILNFLIDVLKNSEGGFKFKNSIVEALIDIVSFVPQSKELALENLCDFIEDCEFNEILVRILHLLGKEGPSAPNPSLYVRHIYNRVVLENSIIRSAAVVALSKFALTKNDPTLYESIISLLKRIANDKDDEVRDRATIALEFIDSARNKDDVIAQNLIESKYFYDIPSLESKLSSYISSNTDSFATAFDVNQVRKFTEDEMKAINLKRKQEQIFNQKSETTLDTTPEAESVPEKRADANSFAGPNLDDHQEDLLATKYADELLSIEQIKPFGQLVNSSRAISLTEPEAEFVVRGVKHLFKDNVVLQFNITNTLTDIALDNVSVVCTPEISDEAELEELFTLQVDRLLPSEEAACYVAFKKLDEIVMEGFLNNLTFTTKEINPDTNEPFDGDEGFQDEYEIDSIFLNAGDYVKSSFTGNFSATFDELPCEEVAVFNIQEDLSIQEVVDKIILNSSCLPVESTQFAPSDSNSHTLKLFGKSALTGSKVALQIKMIKSSKGLALKVHGKGEDSLLCSDLVNGLMQ
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
2Phosphorylation------MSAHTYKKF
------CCCCCCCCC		28.8527717283
7Acetylation-MSAHTYKKFENSTS
-CCCCCCCCCCCCCC		52.7425381059
8AcetylationMSAHTYKKFENSTSG
CCCCCCCCCCCCCCC		47.7122865919
12PhosphorylationTYKKFENSTSGDLPD
CCCCCCCCCCCCCCC		19.4220377248
14PhosphorylationKKFENSTSGDLPDKM
CCCCCCCCCCCCCCE		30.0820377248
72UbiquitinationALFFSISKLFQHQND
HHHHHHHHHHHCCCC		52.2117644757
108UbiquitinationMATSSIMKDVQNGSD
HHHHHHHHHHCCCCC		53.7515699485
118UbiquitinationQNGSDLIKPDAIRSL
CCCCCCCCHHHHHHH		44.1123749301
118AcetylationQNGSDLIKPDAIRSL
CCCCCCCCHHHHHHH		44.1124489116
175PhosphorylationEVTIRRFTNETQEAV
HHEEECCCCCHHHHH		30.2730377154
178PhosphorylationIRRFTNETQEAVLDL
EECCCCCHHHHHHHH		33.5030377154
226AcetylationTDKMALLKLVRHFSE
CCHHHHHHHHHHHHH		45.8724489116
243AcetylationSMKNQLAKVELVKIV
HHHHHHHHHHHHHHH		44.8524489116
336PhosphorylationLNRISMVSPEKIVVC
HHHHHCCCHHHEEEE		20.7828889911
339UbiquitinationISMVSPEKIVVCNPE
HHCCCHHHEEEECHH		44.1517644757
435PhosphorylationGGFKFKNSIVEALID
CCCCCCHHHHHHHHH		28.7122369663
445PhosphorylationEALIDIVSFVPQSKE
HHHHHHHHHCCCCHH		22.3622369663
450PhosphorylationIVSFVPQSKELALEN
HHHHCCCCHHHHHHH		23.2522369663
480AcetylationRILHLLGKEGPSAPN
HHHHHHCCCCCCCCC		60.5124489116
504PhosphorylationNRVVLENSIIRSAAV
CHHHHCCHHHHHHHH		15.2628152593
525PhosphorylationALTKNDPTLYESIIS
HCCCCCHHHHHHHHH		44.8521551504
527PhosphorylationTKNDPTLYESIISLL
CCCCHHHHHHHHHHH		15.3121551504
529PhosphorylationNDPTLYESIISLLKR
CCHHHHHHHHHHHHH		16.2121551504
541AcetylationLKRIANDKDDEVRDR
HHHHHCCCCHHHHHH		67.8724489116
562UbiquitinationFIDSARNKDDVIAQN
HHHHHCCCCCHHHHH		50.1517644757
562AcetylationFIDSARNKDDVIAQN
HHHHHCCCCCHHHHH		50.1524489116
574UbiquitinationAQNLIESKYFYDIPS
HHHHHHHCCCCCCCC		26.9617644757
581PhosphorylationKYFYDIPSLESKLSS
CCCCCCCCHHHHHHH		45.1428152593
584PhosphorylationYDIPSLESKLSSYIS
CCCCCHHHHHHHHHC		44.1628152593
599PhosphorylationSNTDSFATAFDVNQV
CCCCCCCCCCCHHHH		26.3328889911
610PhosphorylationVNQVRKFTEDEMKAI
HHHHHHCCHHHHHHH		45.6328889911
622UbiquitinationKAINLKRKQEQIFNQ
HHHHHHHHHHHHHCC		57.5123749301
630UbiquitinationQEQIFNQKSETTLDT
HHHHHCCCCCCCCCC		51.9015699485
631PhosphorylationEQIFNQKSETTLDTT
HHHHCCCCCCCCCCC		30.3429136822
633PhosphorylationIFNQKSETTLDTTPE
HHCCCCCCCCCCCCC		39.4929136822
634PhosphorylationFNQKSETTLDTTPEA
HCCCCCCCCCCCCCH		20.7029136822
637PhosphorylationKSETTLDTTPEAESV
CCCCCCCCCCCHHCC		47.5722369663
638PhosphorylationSETTLDTTPEAESVP
CCCCCCCCCCHHCCC		20.8522369663
643PhosphorylationDTTPEAESVPEKRAD
CCCCCHHCCCHHHCC		50.4421551504
647AcetylationEAESVPEKRADANSF
CHHCCCHHHCCCCCC		46.9824489116
647UbiquitinationEAESVPEKRADANSF
CHHCCCHHHCCCCCC		46.9823749301
653PhosphorylationEKRADANSFAGPNLD
HHHCCCCCCCCCCCC		20.4222369663
669PhosphorylationHQEDLLATKYADELL
HHHHHHHHHHHHHCC		25.2626447709
677PhosphorylationKYADELLSIEQIKPF
HHHHHCCCHHHCCCH		36.3821551504
695PhosphorylationVNSSRAISLTEPEAE
CCCCCCCCCCCCCHH		28.4025752575
772UbiquitinationAACYVAFKKLDEIVM
HHHHHHHHHHHHHHH		42.5617644757
773UbiquitinationACYVAFKKLDEIVME
HHHHHHHHHHHHHHH		55.5017644757
791UbiquitinationNNLTFTTKEINPDTN
HCCEEECCEECCCCC		54.2417644757
861UbiquitinationSIQEVVDKIILNSSC
CHHHHHHHHHHCCCC		21.7517644757
887UbiquitinationDSNSHTLKLFGKSAL
CCCCCCEEECCCHHH		42.8117644757
904AcetylationSKVALQIKMIKSSKG
CCHHHHHEEHHCCCC		22.9324489116
907UbiquitinationALQIKMIKSSKGLAL
HHHHEEHHCCCCEEE		45.2222817900
909PhosphorylationQIKMIKSSKGLALKV
HHEEHHCCCCEEEEE		26.2427017623
910UbiquitinationIKMIKSSKGLALKVH
HEEHHCCCCEEEEEE		66.1023749301
915UbiquitinationSSKGLALKVHGKGED
CCCCEEEEEECCCCC		26.9522817900
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 COPG_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPG_YEAST !!
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 COPG_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DUG2_YEASTDUG2physical
10688190
GLO3_YEASTGLO3physical
15254269
EMP47_YEASTEMP47physical
9813082
BOS1_YEASTBOS1physical
9813082
OCH1_YEASTOCH1physical
9813082
SEC22_YEASTSEC22physical
9813082
BET1_YEASTBET1genetic
2192256
EMP24_YEASTEMP24genetic
12925749
GEA2_YEASTGEA2genetic
11294905
MST27_YEASTMST27genetic
12925749
COPB_YEASTSEC26genetic
7929113
EIF3I_YEASTTIF34physical
16554755
SEC2_YEASTSEC2physical
16554755
YP117_YEASTYPR117Wphysical
16554755
ATC1_YEASTPMR1genetic
1379856
RBD2_YEASTRBD2physical
18467557
COPZ_YEASTRET3physical
18467557
SSB1_YEASTSSB1physical
19536198
GEA1_YEASTGEA1physical
19039328
EMP24_YEASTEMP24genetic
18283113
TMEDA_YEASTERV25genetic
18283113
SLY1_YEASTSLY1genetic
1903839
SEC22_YEASTSEC22genetic
1903839
BET1_YEASTBET1genetic
1903839
SLY41_YEASTSLY41genetic
1903839
GLO3_YEASTGLO3physical
14690497
GEA1_YEASTGEA1genetic
11294905
COPB_YEASTSEC26physical
21435344
COPA_YEASTCOP1physical
21435344
COPE_YEASTSEC28physical
21435344
COPB2_YEASTSEC27physical
21435344
COPD_YEASTRET2physical
21435344
VPS1_YEASTVPS1genetic
23891562
VPS8_YEASTVPS8genetic
23891562
VPS21_YEASTVPS21genetic
23891562
ERG3_YEASTERG3genetic
23891562
TR120_YEASTTRS120physical
21813735
RPN5_YEASTRPN5genetic
27708008
PDC2_YEASTPDC2genetic
27708008
GPI19_YEASTGPI19genetic
27708008
MOB2_YEASTMOB2genetic
27708008
NOC3_YEASTNOC3genetic
27708008
BRX1_YEASTBRX1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
ATG15_YEASTATG15genetic
27708008
SLX5_YEASTSLX5genetic
27708008
CRD1_YEASTCRD1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
PEX5_YEASTPEX5genetic
27708008
SKN1_YEASTSKN1genetic
27708008
CSK21_YEASTCKA1genetic
27708008
HOS4_YEASTHOS4genetic
27708008
YPS3_YEASTYPS3genetic
27708008
ELO3_YEASTELO3genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
DCAM_YEASTSPE2genetic
27708008
YO075_YEASTYOL075Cgenetic
27708008
INO4_YEASTINO4genetic
27708008
LEO1_YEASTLEO1genetic
27708008
SUCA_YEASTLSC1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
UBA3_YEASTUBA3genetic
27708008
SPEE_YEASTSPE3genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COPG_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504; SER-581; THR-637;THR-638; SER-653 AND SER-695, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-637; THR-638 ANDSER-653, AND MASS SPECTROMETRY.

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