SC31A_HUMAN - dbPTM
SC31A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC31A_HUMAN
UniProt AC O94979
Protein Name Protein transport protein Sec31A
Gene Name SEC31A
Organism Homo sapiens (Human).
Sequence Length 1220
Subcellular Localization Cytoplasm. Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Endoplasmic reticulum membrane
Peripheral membrane protein. Associates with membranes in a GTP-dependent manner..
Protein Description Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). [PubMed: 10788476 The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity]
Protein Sequence MKLKEVDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPYKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQNDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRISVYSIMGGSTDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTAQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVRMPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKKIDASQTEFEKNVWSFLKVNFEDDSRGKYLELLGYRKEDLGKKIALALNKVDGANVALKDSDQVAQSDGEESPAAEEQLLGEHIKEEKEESEFLPSSGGTFNISVSGDIDGLITQALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLARTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGTRLENEGDSLLQTQACLCYICAGNVEKLVACWTKAQDGSHPLSLQDLIEKVVILRKAVQLTQAMDTSTVGVLLAAKMSQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSNAYPNTPYISSASSYTGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPASQRTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPVPLSSQSSFPQPHLPGGQPFHGVQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLEFLYDKLREQTLSPTITSGLHNIARSIETRNYSEGLTMHTHIVSTSNFSETSAFMPVLKVVLTQANKLGV
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
5 (in isoform 9)Phosphorylation-61.15-
10 (in isoform 9)Phosphorylation-6.76-
14 (in isoform 9)Phosphorylation-6.48-
54PhosphorylationELDLSDPSLDMKSCA
EEECCCCCCCHHHHC		41.8324719451
60S-nitrosocysteinePSLDMKSCATFSSSH
CCCCHHHHCCCCCCC		3.27-
60S-nitrosylationPSLDMKSCATFSSSH
CCCCHHHHCCCCCCC		3.2719483679
78UbiquitinationKLIWGPYKMDSKGDV
EEHHCCCCCCCCCCE		39.09-
101PhosphorylationENGNIILYDPSKIIA
CCCCEEEECHHHEEE		18.5222817900
111UbiquitinationSKIIAGDKEVVIAQN
HHEEECCCEEEEEEC		52.0321890473
111UbiquitinationSKIIAGDKEVVIAQN
HHEEECCCEEEEEEC		52.0321890473
111UbiquitinationSKIIAGDKEVVIAQN
HHEEECCCEEEEEEC		52.0321890473
1112-HydroxyisobutyrylationSKIIAGDKEVVIAQN
HHEEECCCEEEEEEC		52.03-
111UbiquitinationSKIIAGDKEVVIAQN
HHEEECCCEEEEEEC		52.0321890473
111 (in isoform 1)Ubiquitination-52.0321890473
111 (in isoform 2)Ubiquitination-52.0321890473
111 (in isoform 3)Ubiquitination-52.0321890473
111 (in isoform 4)Ubiquitination-52.0321890473
111 (in isoform 5)Ubiquitination-52.0321890473
111 (in isoform 6)Ubiquitination-52.0321890473
111 (in isoform 8)Ubiquitination-52.0321890473
120AcetylationVVIAQNDKHTGPVRA
EEEEECCCCCCCEEE		51.09-
120AcetylationVVIAQNDKHTGPVRA
EEEEECCCCCCCEEE		51.0921466224
120UbiquitinationVVIAQNDKHTGPVRA
EEEEECCCCCCCEEE		51.09-
122PhosphorylationIAQNDKHTGPVRALD
EEECCCCCCCEEEEE		49.2520860994
186PhosphorylationQVQHILASASPSGRA
HHHHHHHHCCCCCCC		26.3225159151
188PhosphorylationQHILASASPSGRATV
HHHHHHCCCCCCCCH		19.6625159151
190PhosphorylationILASASPSGRATVWD
HHHHCCCCCCCCHHC		38.1123186163
206UbiquitinationRKNEPIIKVSDHSNR
CCCCCCEEECCCCCC		36.08-
250PhosphorylationMWDLRFASSPLRVLE
EEEEECCCCHHHHHH		29.7623186163
251PhosphorylationWDLRFASSPLRVLEN
EEEECCCCHHHHHHH		25.2323312004
260 (in isoform 7)Ubiquitination-23.9921890473
270SulfoxidationILAIAWSMADPELLL
HHHHHHHHCCHHHHH		3.2330846556
323PhosphorylationPAVLSAASFDGRISV
HHHEEEEEECCCEEE		24.4821712546
329PhosphorylationASFDGRISVYSIMGG
EEECCCEEEEEECCC		17.4020068231
331PhosphorylationFDGRISVYSIMGGST
ECCCEEEEEECCCCC		5.9120068231
331 (in isoform 2)Phosphorylation-5.91-
331 (in isoform 3)Phosphorylation-5.91-
331 (in isoform 4)Phosphorylation-5.91-
332PhosphorylationDGRISVYSIMGGSTD
CCCEEEEEECCCCCC		12.1620068231
334SulfoxidationRISVYSIMGGSTDGL
CEEEEEECCCCCCHH		4.0130846556
337PhosphorylationVYSIMGGSTDGLRQK
EEEECCCCCCHHHHH		20.0020068231
337 (in isoform 2)Phosphorylation-20.00-
337 (in isoform 3)Phosphorylation-20.00-
337 (in isoform 4)Phosphorylation-20.00-
338PhosphorylationYSIMGGSTDGLRQKQ
EEECCCCCCHHHHHH		37.0420068231
338 (in isoform 2)Phosphorylation-37.04-
338 (in isoform 3)Phosphorylation-37.04-
338 (in isoform 4)Phosphorylation-37.04-
348UbiquitinationLRQKQVDKLSSSFGN
HHHHHHHHHHHCCCC		51.95-
350PhosphorylationQKQVDKLSSSFGNLD
HHHHHHHHHCCCCCC		29.6723663014
350 (in isoform 2)Phosphorylation-29.67-
350 (in isoform 3)Phosphorylation-29.67-
350 (in isoform 4)Phosphorylation-29.67-
351PhosphorylationKQVDKLSSSFGNLDP
HHHHHHHHCCCCCCC		39.8723663014
352PhosphorylationQVDKLSSSFGNLDPF
HHHHHHHCCCCCCCC		33.5223663014
361PhosphorylationGNLDPFGTGQPLPPL
CCCCCCCCCCCCCCC		32.7823663014
374PhosphorylationPLQIPQQTAQHSIVL
CCCCCCCCCCCEEEE		24.0428857561
378PhosphorylationPQQTAQHSIVLPLKK
CCCCCCCEEEEECCC		11.4328857561
380 (in isoform 7)Ubiquitination-5.1621890473
397PhosphorylationIRRPVGASFSFGGKL
CCCCCCCEEEECCEE		18.5923312004
399PhosphorylationRPVGASFSFGGKLVT
CCCCCEEEECCEEEE		22.0823312004
412SulfoxidationVTFENVRMPSHQGAE
EEEECEECCCCCCHH		3.3030846556
442PhosphorylationEKEFLSRSDQLQQAV
HHHHHCCHHHHHHHH		26.7428102081
451O-linked_GlycosylationQLQQAVQSQGFINYC
HHHHHHHHCCHHHHH		26.1823301498
451PhosphorylationQLQQAVQSQGFINYC
HHHHHHHHCCHHHHH		26.1828102081
457PhosphorylationQSQGFINYCQKKIDA
HHCCHHHHHHHCCCC		7.4628102081
460AcetylationGFINYCQKKIDASQT
CHHHHHHHCCCCHHH		48.4026051181
460UbiquitinationGFINYCQKKIDASQT
CHHHHHHHCCCCHHH		48.40-
461AcetylationFINYCQKKIDASQTE
HHHHHHHCCCCHHHH		21.6826051181
461UbiquitinationFINYCQKKIDASQTE
HHHHHHHCCCCHHHH		21.68-
467PhosphorylationKKIDASQTEFEKNVW
HCCCCHHHHHHHHHH		39.90-
471AcetylationASQTEFEKNVWSFLK
CHHHHHHHHHHHHEE		63.2226051181
471MethylationASQTEFEKNVWSFLK
CHHHHHHHHHHHHEE		63.2254416421
471UbiquitinationASQTEFEKNVWSFLK
CHHHHHHHHHHHHEE		63.22-
475PhosphorylationEFEKNVWSFLKVNFE
HHHHHHHHHEEEECC		19.2024719451
486MethylationVNFEDDSRGKYLELL
EECCCCCCCCEEHHC		53.25115493567
488UbiquitinationFEDDSRGKYLELLGY
CCCCCCCCEEHHCCC		45.6221890473
488UbiquitinationFEDDSRGKYLELLGY
CCCCCCCCEEHHCCC		45.6221890473
488UbiquitinationFEDDSRGKYLELLGY
CCCCCCCCEEHHCCC		45.6221890473
488AcetylationFEDDSRGKYLELLGY
CCCCCCCCEEHHCCC		45.6225953088
488UbiquitinationFEDDSRGKYLELLGY
CCCCCCCCEEHHCCC		45.6221890473
488 (in isoform 1)Ubiquitination-45.6221890473
488 (in isoform 2)Ubiquitination-45.6221890473
488 (in isoform 3)Ubiquitination-45.6221890473
488 (in isoform 4)Ubiquitination-45.6221890473
488 (in isoform 5)Ubiquitination-45.6221890473
488 (in isoform 6)Ubiquitination-45.6221890473
488 (in isoform 8)Ubiquitination-45.6221890473
495PhosphorylationKYLELLGYRKEDLGK
CEEHHCCCCHHHHHH		20.62-
503UbiquitinationRKEDLGKKIALALNK
CHHHHHHHHHHHHHC		31.26-
510UbiquitinationKIALALNKVDGANVA
HHHHHHHCCCCCCEE		42.42-
521PhosphorylationANVALKDSDQVAQSD
CCEEECCHHHHHCCC		28.4923927012
521 (in isoform 2)Phosphorylation-28.49-
521 (in isoform 3)Phosphorylation-28.49-
521 (in isoform 8)Phosphorylation-28.4921406692
527PhosphorylationDSDQVAQSDGEESPA
CHHHHHCCCCCCCHH		37.5329255136
527 (in isoform 2)Phosphorylation-37.53-
527 (in isoform 3)Phosphorylation-37.53-
527 (in isoform 8)Phosphorylation-37.5321406692
532PhosphorylationAQSDGEESPAAEEQL
HCCCCCCCHHHHHHH		18.6129255136
532 (in isoform 2)Phosphorylation-18.61-
532 (in isoform 3)Phosphorylation-18.61-
556PhosphorylationEESEFLPSSGGTFNI
HHHCCCCCCCCEEEE		43.70-
557PhosphorylationESEFLPSSGGTFNIS
HHCCCCCCCCEEEEE		39.02-
564 (in isoform 7)Phosphorylation-16.0125839225
608UbiquitinationLAIAGGQELLARTQK
HHHHCHHHHHHHHHH		49.37-
608 (in isoform 4)Ubiquitination-49.3721890473
608 (in isoform 6)Ubiquitination-49.3721890473
620UbiquitinationTQKKYFAKSQSKITR
HHHHHHHCCHHHHHH		38.85-
634SulfoxidationRLITAVVMKNWKEIV
HHHHHHHHHCHHHHH		1.9221406390
638AcetylationAVVMKNWKEIVESCD
HHHHHCHHHHHHHCC		47.1326051181
638UbiquitinationAVVMKNWKEIVESCD
HHHHHCHHHHHHHCC		47.13-
647AcetylationIVESCDLKNWREALA
HHHHCCCCCHHHHHH		41.0126051181
647UbiquitinationIVESCDLKNWREALA
HHHHCCCCCHHHHHH		41.0122358839
647 (in isoform 1)Ubiquitination-41.0121890473
647 (in isoform 2)Ubiquitination-41.0121890473
647 (in isoform 3)Ubiquitination-41.0121890473
647 (in isoform 8)Ubiquitination-41.0121890473
658O-linked_GlycosylationEALAAVLTYAKPDEF
HHHHHHHHHCCHHHH		18.1623301498
661UbiquitinationAAVLTYAKPDEFSAL
HHHHHHCCHHHHHHH		42.46-
666O-linked_GlycosylationYAKPDEFSALCDLLG
HCCHHHHHHHHHHHC		20.4823301498
674O-linked_GlycosylationALCDLLGTRLENEGD
HHHHHHCCCCCCCCC		31.8623301498
690UbiquitinationLLQTQACLCYICAGN
HHHHHHHHHHHHHCC		2.52-
707AcetylationKLVACWTKAQDGSHP
HEEEEEECCCCCCCC		21.3926051181
707UbiquitinationKLVACWTKAQDGSHP
HEEEEEECCCCCCCC		21.39-
729UbiquitinationEKVVILRKAVQLTQA
HHHHHHHHHHHHHHH		49.84-
760 (in isoform 4)Phosphorylation-40.33-
765 (in isoform 4)Phosphorylation-11.01-
799PhosphorylationEPVAGHESPKIPYEK
CCCCCCCCCCCCHHH		26.3129255136
799 (in isoform 2)Phosphorylation-26.31-
799 (in isoform 3)Phosphorylation-26.31-
799 (in isoform 8)Phosphorylation-26.3121406692
801UbiquitinationVAGHESPKIPYEKQQ
CCCCCCCCCCHHHCC		66.64-
804PhosphorylationHESPKIPYEKQQLPK
CCCCCCCHHHCCCCC		38.9522167270
804 (in isoform 2)Phosphorylation-38.95-
804 (in isoform 3)Phosphorylation-38.95-
806AcetylationSPKIPYEKQQLPKGR
CCCCCHHHCCCCCCC		37.1826822725
806UbiquitinationSPKIPYEKQQLPKGR
CCCCCHHHCCCCCCC		37.18-
823SulfoxidationPVAGHHQMPRVQTQQ
CCCCCCCCCCCCEEC		1.6730846556
831PhosphorylationPRVQTQQYYPHGENP
CCCCEECCCCCCCCC		14.78-
894DimethylationTGGSAMYRPQQPVAP
CCCCCCCCCCCCCCC		14.96-
894MethylationTGGSAMYRPQQPVAP
CCCCCCCCCCCCCCC		14.9652717285
903O-linked_GlycosylationQQPVAPPTSNAYPNT
CCCCCCCCCCCCCCC		33.2923301498
904O-linked_GlycosylationQPVAPPTSNAYPNTP
CCCCCCCCCCCCCCC		25.8223301498
910O-linked_GlycosylationTSNAYPNTPYISSAS
CCCCCCCCCCCCCCC		16.9923301498
914O-linked_GlycosylationYPNTPYISSASSYTG
CCCCCCCCCCCCCCC		17.6323301498
915O-linked_GlycosylationPNTPYISSASSYTGQ
CCCCCCCCCCCCCCC		23.7023301498
917O-linked_GlycosylationTPYISSASSYTGQSQ
CCCCCCCCCCCCCHH		26.3123301498
933PhosphorylationYAAQHQASSPTSSPA
HCHHHHCCCCCCCCC		30.2226074081
934PhosphorylationAAQHQASSPTSSPAT
CHHHHCCCCCCCCCC		34.9026074081
936PhosphorylationQHQASSPTSSPATSF
HHHCCCCCCCCCCCC		43.7326074081
937PhosphorylationHQASSPTSSPATSFP
HHCCCCCCCCCCCCC		37.3926074081
938O-linked_GlycosylationQASSPTSSPATSFPP
HCCCCCCCCCCCCCC		22.4923301498
938PhosphorylationQASSPTSSPATSFPP
HCCCCCCCCCCCCCC		22.4926074081
941PhosphorylationSPTSSPATSFPPPPS
CCCCCCCCCCCCCCC		33.9926074081
948O-linked_GlycosylationTSFPPPPSSGASFQH
CCCCCCCCCCCCCCC		47.3723301498
963O-linked_GlycosylationGGPGAPPSSSAYALP
CCCCCCCCCCCCCCC		35.5523301498
964O-linked_GlycosylationGPGAPPSSSAYALPP
CCCCCCCCCCCCCCC		25.4323301498
965O-linked_GlycosylationPGAPPSSSAYALPPG
CCCCCCCCCCCCCCC		29.6323301498
966 (in isoform 7)Ubiquitination-8.7921890473
989PhosphorylationELPASQRTGPQNGWN
CCCHHHCCCCCCCCC		45.64-
1007 (in isoform 3)Phosphorylation-52.10-
1008 (in isoform 3)Phosphorylation-61.50-
1041O-linked_GlycosylationQMLQQQPSAPVPLSS
HHHHCCCCCCCCCCC		40.6523301498
1047O-linked_GlycosylationPSAPVPLSSQSSFPQ
CCCCCCCCCCCCCCC		21.9123301498
1047 (in isoform 3)Phosphorylation-21.91-
1048O-linked_GlycosylationSAPVPLSSQSSFPQP
CCCCCCCCCCCCCCC		41.5923301498
1049 (in isoform 3)Phosphorylation-39.45-
1050O-linked_GlycosylationPVPLSSQSSFPQPHL
CCCCCCCCCCCCCCC		35.5723301498
1051O-linked_GlycosylationVPLSSQSSFPQPHLP
CCCCCCCCCCCCCCC		33.0523301498
1051 (in isoform 3)Phosphorylation-33.05-
1056UbiquitinationQSSFPQPHLPGGQPF
CCCCCCCCCCCCCCC		39.13-
1064 (in isoform 6)Ubiquitination-42.0421890473
1066UbiquitinationGGQPFHGVQQPLGQT
CCCCCCCCCCCCCCC		3.43-
1073O-linked_GlycosylationVQQPLGQTGMPPSFS
CCCCCCCCCCCCCCC		33.3823301498
1078PhosphorylationGQTGMPPSFSKPNIE
CCCCCCCCCCCCCCC		35.9624719451
1082 (in isoform 4)Phosphorylation-45.92-
1083 (in isoform 4)Phosphorylation-48.99-
1086UbiquitinationFSKPNIEGAPGAPIG
CCCCCCCCCCCCCCC		33.02-
1101PhosphorylationNTFQHVQSLPTKKIT
CHHHHHHCCCCCCCC		34.9225159151
1103 (in isoform 3)Ubiquitination-47.6321890473
1104PhosphorylationQHVQSLPTKKITKKP
HHHHCCCCCCCCCCC		50.7122964224
1105AcetylationHVQSLPTKKITKKPI
HHHCCCCCCCCCCCC		39.9923954790
1105UbiquitinationHVQSLPTKKITKKPI
HHHCCCCCCCCCCCC		39.99-
1106 (in isoform 2)Phosphorylation-59.07-
1107 (in isoform 2)Phosphorylation-7.91-
1108PhosphorylationSLPTKKITKKPIPDE
CCCCCCCCCCCCCCH		41.7324719451
1110UbiquitinationPTKKITKKPIPDEHL
CCCCCCCCCCCCHHE		39.26-
1120UbiquitinationPDEHLILKTTFEDLI
CCHHEEEECCHHHHH		38.23-
1121PhosphorylationDEHLILKTTFEDLIQ
CHHEEEECCHHHHHH		33.0220068231
1122PhosphorylationEHLILKTTFEDLIQR
HHEEEECCHHHHHHH		24.3620068231
1122 (in isoform 4)Phosphorylation-24.36-
1124 (in isoform 4)Phosphorylation-50.22-
1126 (in isoform 4)Phosphorylation-2.57-
1130S-nitrosylationFEDLIQRCLSSATDP
HHHHHHHHHHCCCCH		2.1824105792
1140UbiquitinationSATDPQTKRKLDDAS
CCCCHHHHHHHHHHH		42.14-
1146 (in isoform 2)Phosphorylation-19.33-
1148 (in isoform 2)Phosphorylation-63.82-
1150 (in isoform 2)Phosphorylation-6.66-
1154PhosphorylationSKRLEFLYDKLREQT
HHHHHHHHHHHHHCC		19.16-
11562-HydroxyisobutyrylationRLEFLYDKLREQTLS
HHHHHHHHHHHCCCC		35.57-
1156UbiquitinationRLEFLYDKLREQTLS
HHHHHHHHHHHCCCC		35.57-
1161PhosphorylationYDKLREQTLSPTITS
HHHHHHCCCCHHHHH		25.1729255136
1163UbiquitinationKLREQTLSPTITSGL
HHHHCCCCHHHHHHH		24.31-
1163PhosphorylationKLREQTLSPTITSGL
HHHHCCCCHHHHHHH		24.3129255136
1165PhosphorylationREQTLSPTITSGLHN
HHCCCCHHHHHHHHH		33.2522167270
1167PhosphorylationQTLSPTITSGLHNIA
CCCCHHHHHHHHHHH		21.1530266825
1168PhosphorylationTLSPTITSGLHNIAR
CCCHHHHHHHHHHHH		35.1930266825
1176 (in isoform 8)Phosphorylation-18.7621406692
1178 (in isoform 4)Ubiquitination-42.8521890473
1182PhosphorylationRSIETRNYSEGLTMH
HHHHCCCCCCCCEEE		12.57-
1202 (in isoform 2)Ubiquitination-18.5621890473
1213PhosphorylationPVLKVVLTQANKLGV
HHHHHHHHHHHHHCC		17.6424275569
1217AcetylationVVLTQANKLGV----
HHHHHHHHHCC----		50.0325953088
1217MalonylationVVLTQANKLGV----
HHHHHHHHHCC----		50.0326320211
1217UbiquitinationVVLTQANKLGV----
HHHHHHHHHCC----		50.0322358839
1217 (in isoform 1)Ubiquitination-50.0321890473
1230 (in isoform 8)Ubiquitination-21890473
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
-KUbiquitinationE3 ubiquitin ligaseKLHL12Q53G59
PMID:22358839
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC31A_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 SC31A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAM2_HUMANSTAM2physical
19054391
SEC13_HUMANSEC13physical
22939629
ARMT1_HUMANC6orf211physical
26344197
VATC1_HUMANATP6V1C1physical
26344197
ENOG_HUMANENO2physical
26344197
FPPS_HUMANFDPSphysical
26344197
NUD13_HUMANNUDT13physical
26344197
SEC13_HUMANSEC13physical
26344197
SC23A_HUMANSEC23Aphysical
26344197
SC23B_HUMANSEC23Bphysical
26344197
SC24B_HUMANSEC24Bphysical
26344197
ELOB_HUMANTCEB2physical
26344197
SCYL1_HUMANSCYL1physical
28514442
TFG_HUMANTFGphysical
28514442
SEC13_HUMANSEC13physical
28514442
NOP14_HUMANNOP14physical
28514442
S23IP_HUMANSEC23IPphysical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
GRDN_HUMANCCDC88Aphysical
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 SC31A_HUMAN

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Related Literatures of Post-Translational Modification
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-799 AND SER-1163, ANDMASS 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-527; SER-532; SER-799AND THR-1161, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Ubiquitin-dependent regulation of COPII coat size and function.";
Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C.,Schekman R., Rape M.;
Nature 482:495-500(2012).
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217,MUTAGENESIS OF LYS-647 AND LYS-1217, AND INTERACTION WITH KLHL12.

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