THS7A_HUMAN - dbPTM
THS7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THS7A_HUMAN
UniProt AC Q9UPZ6
Protein Name Thrombospondin type-1 domain-containing protein 7A
Gene Name THSD7A
Organism Homo sapiens (Human).
Sequence Length 1657
Subcellular Localization Thrombospondin type-1 domain-containing protein 7A: Cell membrane
Single-pass type I membrane protein . Cell projection . Detected on podocyte foot processes.
Thrombospondin type-1 domain-containing protein 7A, soluble form: Secreted . Proteo
Protein Description Thrombospondin type-1 domain-containing protein 7A: Plays a role in actin cytoskeleton rearrangement.; Thrombospondin type-1 domain-containing protein 7A, soluble form: The soluble form promotes endothelial cell migration and filopodia formation during sprouting angiogenesis via a FAK-dependent mechanism..
Protein Sequence MGLQARRWASGSRGAAGPRRGVLQLLPLPLPLPLLLLLLLRPGAGRAAAQGEAEAPTLYLWKTGPWGRCMGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVISKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQVRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKAADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECPEFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANENLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGNCEPDNGKECGPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVICVRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQLPANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCRKQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSEHVEDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAVEKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKYCEALGLEKNWQMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYEYKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEVMSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPDGRLKTWVYGVAAGAFVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
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
10PhosphorylationLQARRWASGSRGAAG
HHHHHHCCCCCCCCC		30.2728634120
12PhosphorylationARRWASGSRGAAGPR
HHHHCCCCCCCCCCC		25.6628634120
234N-linked_GlycosylationFGGSGCPNLTEFQVC
CCCCCCCCCCEEEEE		64.77UniProtKB CARBOHYD
253PhosphorylationCEAEELRYSLHVGPW
CCHHHHHEEEECCCC		28.3623663014
254PhosphorylationEAEELRYSLHVGPWS
CHHHHHEEEECCCCC		12.9323663014
261PhosphorylationSLHVGPWSTCSMPHS
EEECCCCCCCCCCHH		23.7523663014
262PhosphorylationLHVGPWSTCSMPHSR
EECCCCCCCCCCHHH		12.5323663014
264PhosphorylationVGPWSTCSMPHSRQV
CCCCCCCCCCHHHHH		35.1223663014
268PhosphorylationSTCSMPHSRQVRQAR
CCCCCCHHHHHHHHH		20.6623663014
269MethylationTCSMPHSRQVRQARR
CCCCCHHHHHHHHHH		35.66115389439
323PhosphorylationYWDIQIGYQTREVMC
CCCEEEECEECEEEE		14.35-
332N-linked_GlycosylationTREVMCINKTGKAAD
ECEEEEECCCCCCCC		30.80UniProtKB CARBOHYD
370PhosphorylationVSEWSEWSPCSKTCH
CCCCCCCCCCCCHHH		16.39-
373PhosphorylationWSEWSPCSKTCHDMV
CCCCCCCCCHHHHCC		34.09-
399PhosphorylationIRQFPIGSEKECPEF
EEECCCCCCCCCCCC		46.3324719451
450N-linked_GlycosylationQQDKRRGNQTALCGG
HHHHHCCCCCCCCCC		33.93UniProtKB CARBOHYD
500N-linked_GlycosylationLCTGPIPNTTQLCHI
ECCCCCCCCCEECCC		57.38UniProtKB CARBOHYD
638PhosphorylationCPKDCVLSTWSTWSS
CCCCCEEECCCCCCC		13.87-
654PhosphorylationSHTCSGKTTEGKQIR
CCCCCCCCCCCCEEE		33.3427794612
655PhosphorylationHTCSGKTTEGKQIRA
CCCCCCCCCCCEEEH		46.3427794612
679N-linked_GlycosylationEGGIRCPNSSALQEV
CCCCCCCCCHHHHHH		52.82UniProtKB CARBOHYD
717N-linked_GlycosylationDTSVSSFNTTTTWNG
CCCCCEEECCCEECC		38.16UniProtKB CARBOHYD
734PhosphorylationSCSVGMQTRKVICVR
EEECCCCCCEEEEEE		24.46-
792PhosphorylationSSCKEGDSSIRKQSR
CCCCCCCCCHHHHCC		38.22-
793PhosphorylationSCKEGDSSIRKQSRH
CCCCCCCCHHHHCCC		31.02-
968N-linked_GlycosylationYNAQPVGNWSDCILP
CCCCCCCCHHHEECC		35.00UniProtKB CARBOHYD
1015PhosphorylationQNGRLVETSRCNSHG
CCCCEEEEECCCCCC		17.6230576142
1016PhosphorylationNGRLVETSRCNSHGY
CCCEEEEECCCCCCC		22.7230576142
1034PhosphorylationACIIPCPSDCKLSEW
EEEEECCCCCCHHHC		63.4630576142
1043N-linked_GlycosylationCKLSEWSNWSRCSKS
CCHHHCCCCCHHHCC		41.64UniProtKB CARBOHYD
1045PhosphorylationLSEWSNWSRCSKSCG
HHHCCCCCHHHCCCC		27.8824719451
1048PhosphorylationWSNWSRCSKSCGSGV
CCCCCHHHCCCCCCC		26.8822964224
1050PhosphorylationNWSRCSKSCGSGVKV
CCCHHHCCCCCCCEE		13.8630631047
1053PhosphorylationRCSKSCGSGVKVRSK
HHHCCCCCCCEECCH		44.7522964224
1182N-linked_GlycosylationTQCVLPCNQSSFRQR
CEEEEECCCHHHHCC		42.71UniProtKB CARBOHYD
1220PhosphorylationCNLNKNCYHYDYNVT
CCCCCCCEEECCCCC		16.8924043423
1222PhosphorylationLNKNCYHYDYNVTDW
CCCCCEEECCCCCCC		8.1424043423
1224PhosphorylationKNCYHYDYNVTDWST
CCCEEECCCCCCCCC		12.3624043423
1225N-linked_GlycosylationNCYHYDYNVTDWSTC
CCEEECCCCCCCCCC		27.58UniProtKB CARBOHYD
1227PhosphorylationYHYDYNVTDWSTCQL
EEECCCCCCCCCCCC		28.2824043423
1230PhosphorylationDYNVTDWSTCQLSEK
CCCCCCCCCCCCCCC		23.3224043423
1231PhosphorylationYNVTDWSTCQLSEKA
CCCCCCCCCCCCCCE		10.4624043423
1235PhosphorylationDWSTCQLSEKAVCGN
CCCCCCCCCCEECCC		15.9224043423
1276N-linked_GlycosylationLEKNWQMNTSCMVEC
CCCCEECCCCEEEEE		17.46UniProtKB CARBOHYD
1277PhosphorylationEKNWQMNTSCMVECP
CCCEECCCCEEEEEC		20.2624043423
1278PhosphorylationKNWQMNTSCMVECPV
CCEECCCCEEEEECC		8.6624043423
1290PhosphorylationCPVNCQLSDWSPWSE
ECCCCCCCCCCCHHH		15.9124043423
1293PhosphorylationNCQLSDWSPWSECSQ
CCCCCCCCCHHHHHC		22.8324043423
1296PhosphorylationLSDWSPWSECSQTCG
CCCCCCHHHHHCHHC		31.9124043423
1299PhosphorylationWSPWSECSQTCGLTG
CCCHHHHHCHHCCCC		25.1924043423
1301PhosphorylationPWSECSQTCGLTGKM
CHHHHHCHHCCCCCE		7.7024043423
1305PhosphorylationCSQTCGLTGKMIRRR
HHCHHCCCCCEEEEE		21.7524043423
1341PhosphorylationPCPVKPCYRWQYGQW
CCCCCCCEECCCCCC		24.3417053785
1366N-linked_GlycosylationGEGTRTRNISCVVSD
CCCCCCCEEEEEEEC		29.88UniProtKB CARBOHYD
1368PhosphorylationGTRTRNISCVVSDGS
CCCCCEEEEEEECCC		12.3829514088
1372PhosphorylationRNISCVVSDGSADDF
CEEEEEEECCCCCHH		18.8229514088
1375PhosphorylationSCVVSDGSADDFSKV
EEEEECCCCCHHHHH		33.2529514088
1380PhosphorylationDGSADDFSKVVDEEF
CCCCCHHHHHCCHHH		31.3829514088
1496PhosphorylationRTVWCQRSDGINVTG
CEEEEECCCCEEECC		17.8218452278
1500N-linked_GlycosylationCQRSDGINVTGGCLV
EECCCCEEECCCEEE		30.72UniProtKB CARBOHYD
1547N-linked_GlycosylationYTEVMSSNSTLEQCT
CEEEECCCCCCEECE		31.54UniProtKB CARBOHYD
1580O-linked_GlycosylationTSRAVHPTQPSSNPA
CCCEECCCCCCCCCC		37.93OGP
1645UbiquitinationRRQNNRLKPLTLAYD
CCCCCCCCCCEEEEC		34.4432142685
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 THS7A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THS7A_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 THS7A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASAP2_HUMANASAP2physical
12421765
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 THS7A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1341, AND MASSSPECTROMETRY.

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