TSP2_HUMAN - dbPTM
TSP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSP2_HUMAN
UniProt AC P35442
Protein Name Thrombospondin-2
Gene Name THBS2
Organism Homo sapiens (Human).
Sequence Length 1172
Subcellular Localization
Protein Description Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties..
Protein Sequence MVWRLVLLALWVWPSTQAGHQDKDTTFDLFSISNINRKTIGAKQFRGPDPGVPAYRFVRFDYIPPVNADDLSKITKIMRQKEGFFLTAQLKQDGKSRGTLLALEGPGLSQRQFEIVSNGPADTLDLTYWIDGTRHVVSLEDVGLADSQWKNVTVQVAGETYSLHVGCDLIDSFALDEPFYEHLQAEKSRMYVAKGSARESHFRGLLQNVHLVFENSVEDILSKKGCQQGQGAEINAISENTETLRLGPHVTTEYVGPSSERRPEVCERSCEELGNMVQELSGLHVLVNQLSENLKRVSNDNQFLWELIGGPPKTRNMSACWQDGRFFAENETWVVDSCTTCTCKKFKTICHQITCPPATCASPSFVEGECCPSCLHSVDGEEGWSPWAEWTQCSVTCGSGTQQRGRSCDVTSNTCLGPSIQTRACSLSKCDTRIRQDGGWSHWSPWSSCSVTCGVGNITRIRLCNSPVPQMGGKNCKGSGRETKACQGAPCPIDGRWSPWSPWSACTVTCAGGIRERTRVCNSPEPQYGGKACVGDVQERQMCNKRSCPVDGCLSNPCFPGAQCSSFPDGSWSCGSCPVGFLGNGTHCEDLDECALVPDICFSTSKVPRCVNTQPGFHCLPCPPRYRGNQPVGVGLEAAKTEKQVCEPENPCKDKTHNCHKHAECIYLGHFSDPMYKCECQTGYAGDGLICGEDSDLDGWPNLNLVCATNATYHCIKDNCPHLPNSGQEDFDKDGIGDACDDDDDNDGVTDEKDNCQLLFNPRQADYDKDEVGDRCDNCPYVHNPAQIDTDNNGEGDACSVDIDGDDVFNERDNCPYVYNTDQRDTDGDGVGDHCDNCPLVHNPDQTDVDNDLVGDQCDNNEDIDDDGHQNNQDNCPYISNANQADHDRDGQGDACDPDDDNDGVPDDRDNCRLVFNPDQEDLDGDGRGDICKDDFDNDNIPDIDDVCPENNAISETDFRNFQMVPLDPKGTTQIDPNWVIRHQGKELVQTANSDPGIAVGFDEFGSVDFSGTFYVNTDRDDDYAGFVFGYQSSSRFYVVMWKQVTQTYWEDQPTRAYGYSGVSLKVVNSTTGTGEHLRNALWHTGNTPGQVRTLWHDPRNIGWKDYTAYRWHLTHRPKTGYIRVLVHEGKQVMADSGPIYDQTYAGGRLGLFVFSQEMVYFSDLKYECRDI
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
16PhosphorylationALWVWPSTQAGHQDK
HHHHCCCCCCCCCCC		20.5426437602
109PhosphorylationALEGPGLSQRQFEIV
EEECCCCCHHHEEEE		29.27-
151N-linked_GlycosylationLADSQWKNVTVQVAG
CCCCCCCCEEEEECC		31.56UniProtKB CARBOHYD
238PhosphorylationGAEINAISENTETLR
CCEEEEEECCCCCEE		23.5324505115
241PhosphorylationINAISENTETLRLGP
EEEEECCCCCEECCC		26.7122210691
243PhosphorylationAISENTETLRLGPHV
EEECCCCCEECCCCC		18.3622210691
251O-linked_GlycosylationLRLGPHVTTEYVGPS
EECCCCCEECCCCCC		15.7555832885
252PhosphorylationRLGPHVTTEYVGPSS
ECCCCCEECCCCCCC		24.9922210691
252O-linked_GlycosylationRLGPHVTTEYVGPSS
ECCCCCEECCCCCCC		24.9955832891
258PhosphorylationTTEYVGPSSERRPEV
EECCCCCCCCCCHHH		38.6124505115
259PhosphorylationTEYVGPSSERRPEVC
ECCCCCCCCCCHHHH		37.9528857561
259O-linked_GlycosylationTEYVGPSSERRPEVC
ECCCCCCCCCCHHHH		37.9555832897
316N-linked_GlycosylationGGPPKTRNMSACWQD
CCCCCCCCCHHHCCC		33.71UniProtKB CARBOHYD
318PhosphorylationPPKTRNMSACWQDGR
CCCCCCCHHHCCCCC		24.67-
330N-linked_GlycosylationDGRFFAENETWVVDS
CCCEEECCCEEEEEC		48.87UniProtKB CARBOHYD
332PhosphorylationRFFAENETWVVDSCT
CEEECCCEEEEECCC		34.83-
399PhosphorylationQCSVTCGSGTQQRGR
EEEEECCCCCCCCCC		40.59-
401PhosphorylationSVTCGSGTQQRGRSC
EEECCCCCCCCCCCC		24.19-
457N-linked_GlycosylationSVTCGVGNITRIRLC
EEEECCCCEEEEEEE		30.01UniProtKB CARBOHYD
479PhosphorylationGGKNCKGSGRETKAC
CCCCCCCCCCCCCCC		21.8521060948
584N-linked_GlycosylationCPVGFLGNGTHCEDL
CCEEECCCCCCCCCH		55.1016186819
710N-linked_GlycosylationLNLVCATNATYHCIK
CEEEEECCCEEEHHH		16.2616186819
1024PhosphorylationNTDRDDDYAGFVFGY
CCCCCCCCEEEEEEE		18.67-
1031PhosphorylationYAGFVFGYQSSSRFY
CEEEEEEEECCCEEE		8.18-
1035PhosphorylationVFGYQSSSRFYVVMW
EEEEECCCEEEEEEE		31.49-
1038PhosphorylationYQSSSRFYVVMWKQV
EECCCEEEEEEEEEC		7.33-
1069N-linked_GlycosylationGVSLKVVNSTTGTGE
CCEEEEEECCCCCCH		36.3016186819
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 TSP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSP2_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 TSP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MMP2_HUMANMMP2physical
10900205
TSP1_HUMANTHBS1physical
28514442
D19L3_HUMANDPY19L3physical
28514442
B3GLT_HUMANB3GALTLphysical
28514442
ZWINT_HUMANZWINTphysical
28514442
PPR21_HUMANPPP1R21physical
28514442
PIGA_HUMANPIGAphysical
28514442
AP1G2_HUMANAP1G2physical
28514442
EDEM2_HUMANEDEM2physical
28514442
FOXF2_HUMANFOXF2physical
28514442
ZN696_HUMANZNF696physical
28514442
D19L1_HUMANDPY19L1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603932Intervertebral disc disease (IDD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TSP2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of the calcium-rich signature domain of humanthrombospondin-2.";
Carlson C.B., Bernstein D.A., Annis D.S., Misenheimer T.M.,Hannah B.L., Mosher D.F., Keck J.L.;
Nat. Struct. Mol. Biol. 12:910-914(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 551-1172 IN COMPLEX WITHCALCIUM IONS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-584; ASN-710AND ASN-1069.

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