SPTCA_DROME - dbPTM
SPTCA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPTCA_DROME
UniProt AC P13395
Protein Name Spectrin alpha chain
Gene Name alpha-Spec
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2415
Subcellular Localization Cytoplasm, cytoskeleton . Golgi apparatus . Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi.
Protein Description Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization..
Protein Sequence MENFTPKEVKILETVEDIQERREQVLSRYNDFKIETRQKREKLEDSRRFQYFKRDADELESWIHEKLQAASEESYRDPTNLQAKIQKHQAFEAEVSAHSNAIVSLDNTGQEMINQQHFASESIQVRLDELHKLWELLLSRLAEKGLKLQQALVLVQFLRQCEEVMFWIKDKETFVTADEFGQDLEHVEVLQRKFDEFQKDMASQEYRVTEVNQLADKLVQDGHPERDTITKRKEELNEAWQRLKQLAIVRQEKLFGAHEIQRFNRDADETVAWIAEKDVVLSSDDYGRDLASVQALQRKHEGVERDLAALEDKVSTLGAEAQRLCSIHADHSDQIRDKQAEIANYWQSLTTKARERKQKLDESYYLHRFLADFRDLVSWINGMKAIISADELAKDVAGAEALLERHQEHKGEIDAREDSFKLTTESGQKLLEREHYAAAEIQEKLAALENDKSSLLSLWEDRRILYEQCMDLQLFYRDTEQADTWMAKQEAFLANEDLGDSLDSVEALIKKHEDFEKSLAAQEEKIKALDIFATKLIDGQHYAADDVAQRRQMLLARRAALQEKSSKRRQLLEDSNRYQQFERDCDETKGWISEKLKFATDDSYLDPTNLNGKMQKHQNFEHELNANKSRIEDITNVGTELIEKQHYAADQINTRMQEIVVLWETLVQASDKKGTKLNEACQQQQFNRTIEDIELWLSEIEGQLLSEDHGKDLTSVQNLQKKHALLEADVMAHQDRIESIKVAANKFIESGHFDADNIRNKEGNLSARYAALAAPMGERKQHLLDSLQVQQLFRDLEDEAAWIREKEPIAASTNRGRDLIGVQNLIKKHQAVLAEINNHEARLLNVISSGENMLKDQPFASDDIRQRLEALQEQWNTLKEKSSQRKQDLDDSLQAHQYFADANEAESWMREKEPIATGSDYGKDEDSSEALLKKHEALVSDLEAFGNTIQALQEQAKNCRQQETPVVDITGKECVVALYDYTEKSPREVSMKKGDVLTLLNSNNKDWWKVEVNDRQGFVPAAYIKKIDAGLSASQQNLVDNHSIAKRQNQINSQYDNLLALARERQNKLNETVKAYVLVREAADLAQWIRDKENHAQIADVVGEDLEEVEVLQKKFDDFNDDLKANEVRLANMNEIAVQLTSLGQTEAALKIQTQMQDLNEKWNNLQTLTAEKASQLGSAHEVQRFHRDIDETKDWIAEKANALNNDDLGKDLRSVQTLQRKHEGVERDLAALRDKIRQLDETANRLMQSHPDTAEQTYAKQKEINEMWDQIITKSTARKEKLLDSYDLQRFLSDYRDLLAWINSMMSLVTSDELANDVTGAEALIERHQEHRTEIDARAGTFGAFEQFGNELLQANHYASPEIKEKIEDLAKAREDLEKAWTERRLQLEQNLDLQLYMRDCELAESWMSAREAFLNADDDANAGGNVEALIKKHEDFDKAINGHEQKIAALQTVADQLIAQNHYASNLVDEKRKQVLERWRHLKEGLIEKRSRLGDEQTLQQFSRDADEIENWIAEKLQLATEESYKDPANIQSKHQKHQAFEAELAANADRIQSVLAMGGNLIDKKQCSGSEDAVQKRLTQIADQWEYLTHKTTEKSLKLKEANKQRTYIAAVKDLDFWLGEVESLLTTEDSGKDLASVQNLMKKHQLVEADIVAHEDRIKDMNNQADSLVESGQFDTAGIQEKRQSINERYERICNLAAHRQARLNEALTLHQFFRDIADEESWIKEKKLLVGSDDYGRDLTGVQNLKKKHKRLEAELGSHEPAIQAVQEAGEKLMDVSNLGVPEIEQRLKALNQAWAELKNLAATRGQKLDESLTYQQFLAQVEEEEAWITEKQQLLSVEDYGDSMAAVQGLLKKHDAFETDFTAHKDRCSLICDQGSELVEAKNHHGESIAQRCQQLRLKLDNLSALAARRKGALLDNSAYLQFMWKADVVESWIDDKENYVRSDEFGRDLSTVQTLLTKQETFDAGLNAFEQEGIHNITALKDQLINASHAQSPAILKRHGDVIARWQKLRDASNTRKDRLLAMQEQFRQIEELYLTFAKKASAFNSWFENAEEDLTDPVRCNSIEEIRALRDAHAQFQASLSSAEADFKALAALDQKIKSFNVGPNPYTWFTMEALEETWRNLQKIIEERDGELAKEAKRQEENDKLRKEFAKHANLFHQWLTETRTSMMEGSGSLEQQLEALRVKATEVRARRVDLKKIEELGALLEEHLILDNRYTEHSTVGLAQQWDQLDQLSMRMQHNLEQQIQARNHSGVSEDSLKEFSMMFKHFDKDKSGKLNHQEFKSCLRALGYDLPMVEEGQPDPEFEAILDVVDPNRDGYVSLQEYIAFMISKETENVQSYEEIENAFRAITAADRPYVTKEELYCNLTKDMADYCVQRMKPFSEPRSGQPIKDALDYIDFTRTLFQN
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
848PhosphorylationARLLNVISSGENMLK
HHHHHHHHCCCHHHC		28.1822668510
849PhosphorylationRLLNVISSGENMLKD
HHHHHHHCCCHHHCC		38.7222668510
861PhosphorylationLKDQPFASDDIRQRL
HCCCCCCCHHHHHHH		35.8722668510
917PhosphorylationREKEPIATGSDYGKD
HHCCCCCCCCCCCCC		37.6327794539
964PhosphorylationKNCRQQETPVVDITG
HHHCCCCCCEEECCC		19.6227794539
979PhosphorylationKECVVALYDYTEKSP
CEEEEEEEECCCCCC		9.3625749252
1032PhosphorylationKKIDAGLSASQQNLV
EHHHCCCCHHHHCCC		25.5919429919
1034PhosphorylationIDAGLSASQQNLVDN
HHCCCCHHHHCCCCC		28.9921082442
1218PhosphorylationKDLRSVQTLQRKHEG
HHHHHHHHHHHHCCC		23.7819429919
1407PhosphorylationRDCELAESWMSAREA
HHHHHHHHHHHHHHH		23.5919429919
1582PhosphorylationDAVQKRLTQIADQWE
HHHHHHHHHHHHHHH		23.2019429919
1689PhosphorylationGIQEKRQSINERYER
HHHHHHHHHHHHHHH		31.2622817900
1894PhosphorylationAKNHHGESIAQRCQQ
HHCCCCHHHHHHHHH		28.0222817900
1938PhosphorylationWKADVVESWIDDKEN
HHHHHHHHHHCCCCC		20.0919429919
1968PhosphorylationTLLTKQETFDAGLNA
HHHHHHHHHHHCCHH		25.0727794539
2260PhosphorylationQIQARNHSGVSEDSL
HHHHHCCCCCCHHHH		44.4322817900
2266PhosphorylationHSGVSEDSLKEFSMM
CCCCCHHHHHHHHHH		36.9721082442
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 SPTCA_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPTCA_DROME !!
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 SPTCA_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_DROMETER94physical
22036573
SPTCB_DROMEbeta-Specgenetic
17121810
MIRO_DROMEMirogenetic
22153373
JNK_DROMEbskgenetic
22153373
LVA_DROMElvaphysical
11076973
SPTCB_DROMEbeta-Specphysical
11076973
SPTCB_DROMEbeta-Specphysical
25381248
SPTCB_DROMEbeta-Specphysical
3680372
CL190_DROMECLIP-190physical
11076973
CALM_DROMECamphysical
2016322
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPTCA_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032 AND SER-1034, ANDMASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND MASSSPECTROMETRY.

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